ID ACKA_MYCGE Reviewed; 393 AA. AC P47599; Q49485; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 103. 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}; OrderedLocusNames=MG357; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-114. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate CC and ATP. Can also catalyze the reverse reaction. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020}; CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP- CC Rule:MF_00020}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA CC biosynthesis; acetyl-CoA from acetate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020}. 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; L43967; AAC71582.1; -; Genomic_DNA. DR EMBL; X61531; CAA43743.1; -; Genomic_DNA. DR PIR; E64239; E64239. DR RefSeq; WP_009885814.1; NZ_AAGX01000006.1. DR ProteinModelPortal; P47599; -. DR STRING; 243273.MgenG_010200001928; -. DR EnsemblBacteria; AAC71582; AAC71582; MG_357. DR KEGG; mge:MG_357; -. DR PATRIC; 20010290; VBIMycGen98045_0419. DR eggNOG; ENOG4105C6H; Bacteria. DR eggNOG; COG0282; LUCA. DR KO; K00925; -. DR OMA; DEELMIV; -. DR OrthoDB; EOG69975F; -. DR BioCyc; MGEN243273:GH2R-411-MONOMER; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 393 Acetate kinase. FT /FTId=PRO_0000107586. FT NP_BIND 204 208 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 278 280 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 323 327 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT ACT_SITE 146 146 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT METAL 10 10 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT METAL 376 376 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT BINDING 17 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT BINDING 89 89 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT SITE 178 178 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT SITE 237 237 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT CONFLICT 48 48 Q -> S (in Ref. 2; CAA43743). FT {ECO:0000305}. SQ SEQUENCE 393 AA; 44346 MW; 985CE65FC7B92225 CRC64; MQSHKILVVN AGSSSIKFQL FNDKKQVLAK GLCERIFIDG FFKLEFNQKK IEEKVQFNDH NLAVKHFLNA LKKNKIITEL SEIGLIGHRV VQGANYFTDA VLVDTHSLAK IKEFIKLAPL HNKPEADVIE IFLKEIKTAK NVAVFDTTFH TTIPRENYLY AVPENWEKNN LVRRYGFHGT SYKYINEFLE KKFNKKPLNL IVCHLGNGAS VCAIKQGKSL NTSMGFTPLE GLIMGTRSGD IDPAIVSYIA EQQKLSCNDV VNELNKKSGM FAITGSSDMR DIFDKPEIND IAIKMYVNRV ADYIAKYLNQ LSGEIDSLVF TGGVGENASY CVQLIIEKVA SLGFKTNSNL FGNYQDSSLI STNESKYQIF RVRTNEELMI VEDALRVSTN IKK // ID ACPH_MYCGE Reviewed; 84 AA. AC P47529; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=Acyl carrier protein homolog; DE Short=ACP; GN OrderedLocusNames=MG287; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid CC biosynthesis. {ECO:0000250}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific CC serine of the apo-ACP-like protein. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 acyl carrier domain. {ECO:0000255|PROSITE- CC ProRule:PRU00258}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71509.1; -; Genomic_DNA. DR PIR; G64231; G64231. DR ProteinModelPortal; P47529; -. DR STRING; 243273.MgenG_010200003305; -. DR PRIDE; P47529; -. DR EnsemblBacteria; AAC71509; AAC71509; MG_287. DR KEGG; mge:MG_287; -. DR PATRIC; 20010086; VBIMycGen98045_0330. DR eggNOG; COG0236; LUCA. DR KO; K02078; -. DR OMA; FMEILSV; -. DR OrthoDB; EOG6MWNJM; -. DR BioCyc; MGEN243273:GH2R-321-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.1200.10; -; 1. DR InterPro; IPR003231; Acyl_carrier. DR InterPro; IPR009081; PP-bd_ACP. DR Pfam; PF00550; PP-binding; 1. DR ProDom; PD000887; PD000887; 1. DR SUPFAM; SSF47336; SSF47336; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. PE 3: Inferred from homology; KW Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; KW Phosphoprotein; Reference proteome. FT CHAIN 1 84 Acyl carrier protein homolog. FT /FTId=PRO_0000180265. FT MOD_RES 39 39 O-(pantetheine 4'-phosphoryl)serine. FT {ECO:0000255|PROSITE-ProRule:PRU00258}. SQ SEQUENCE 84 AA; 9643 MW; 7953C8AA030AFD10 CRC64; MQTHEILLKI KEIAKSKNFN LNLDEKTINQ PLRELKIDSL DMFSIVVSLE NEFGISFDDE KLMNLKNLAD LVLEVKNLLA KKGV // ID ACPS_MYCGE Reviewed; 114 AA. AC Q9ZB79; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 98. 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=MG211.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. 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; L43967; AAC71438.1; -; Genomic_DNA. DR RefSeq; WP_009885751.1; NZ_AAGX01000004.1. DR ProteinModelPortal; Q9ZB79; -. DR STRING; 243273.MgenG_010200001422; -. DR EnsemblBacteria; AAC71438; AAC71438; MG_482. DR KEGG; mge:MG_482; -. DR PATRIC; 20009882; VBIMycGen98045_0246. DR eggNOG; COG0736; LUCA. DR KO; K00997; -. DR OrthoDB; EOG6384R9; -. DR BioCyc; MGEN243273:GH2R-223-MONOMER; -. DR Proteomes; UP000000807; 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; 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 1 114 Holo-[acyl-carrier-protein] synthase. FT /FTId=PRO_0000175668. FT METAL 8 8 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00101}. FT METAL 58 58 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00101}. SQ SEQUENCE 114 AA; 13153 MW; 8992BBB560373E92 CRC64; MVVGIGIDVV QLKRFLTLVE TSDCFAKRLL TSNELNSYWK LNNNQRANFL AVHWTLKEAI YKATSHIKPL FTKLEIYKLN NQYRCEFIQN INLLLSVSYT NCHVSAICLA QQNG // ID ALF_MYCGE Reviewed; 288 AA. AC P47269; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Fructose-bisphosphate aldolase; DE Short=FBP aldolase; DE Short=FBPA; DE EC=4.1.2.13; DE AltName: Full=Fructose-1,6-bisphosphate aldolase; GN Name=fba; Synonyms=tsr; OrderedLocusNames=MG023; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3- CC phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in CC gluconeogenesis and the reverse reaction in glycolysis. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone CC phosphate + D-glyceraldehyde 3-phosphate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the CC other provides a structural contribution. {ECO:0000250}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase 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; L43967; AAC71239.1; -; Genomic_DNA. DR PIR; E64202; E64202. DR RefSeq; WP_009885917.1; NZ_AAGX01000010.1. DR ProteinModelPortal; P47269; -. DR STRING; 243273.MgenG_010200002766; -. DR EnsemblBacteria; AAC71239; AAC71239; MG_023. DR KEGG; mge:MG_023; -. DR PATRIC; 20009422; VBIMycGen98045_0021. DR eggNOG; ENOG4105D2N; Bacteria. DR eggNOG; COG0191; LUCA. DR KO; K01624; -. DR OMA; GGTEDHI; -. DR OrthoDB; EOG6HXJ7B; -. DR BioCyc; MGEN243273:GH2R-23-MONOMER; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. 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:UniProtKB-UniPathway. 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. DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1. DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Lyase; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1 288 Fructose-bisphosphate aldolase. FT /FTId=PRO_0000178719. FT REGION 207 209 Dihydroxyacetone phosphate binding. FT {ECO:0000250}. FT REGION 228 231 Dihydroxyacetone phosphate binding. FT {ECO:0000250}. FT ACT_SITE 84 84 Proton donor. {ECO:0000250}. FT METAL 85 85 Zinc 1; catalytic. {ECO:0000250}. FT METAL 105 105 Zinc 2. {ECO:0000250}. FT METAL 135 135 Zinc 2. {ECO:0000250}. FT METAL 177 177 Zinc 1; catalytic. {ECO:0000250}. FT METAL 206 206 Zinc 1; catalytic. {ECO:0000250}. FT BINDING 49 49 Glyceraldehyde 3-phosphate. FT {ECO:0000250}. FT BINDING 178 178 Dihydroxyacetone phosphate; via amide FT nitrogen. {ECO:0000250}. SQ SEQUENCE 288 AA; 31310 MW; BD09F4683DD6A32F CRC64; MLVNFKLMLQ KAKLGKYAIP HININNYEWA KAVLTAANQA NSPIIVSVSE GALKYMSGYS VVIPLVKGLI ESLSVKVPVT LHLDHGSYDA CIQALQAGFS SVMFDGSHLP FEENFNKSKK LIEIAQKTNA SVELEVGTIG GEEDGVIGQG ELANVDECKQ IASLKPDALA AGIGNIHGIY PKNWKGLNFP LIETISKITN LPLVLHGGSG ILENDVKKAI SLGICKLNIN TECQLAFAHE IRKYIESNKD LDLNKKGYDP RKLLKEPTQA IVDTCLEKID LCGSRNKA // ID AMPP_MYCGE Reviewed; 354 AA. AC P47566; Q49192; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Putative Xaa-Pro aminopeptidase; DE Short=X-Pro aminopeptidase; DE EC=3.4.11.9; DE AltName: Full=Aminoacylproline aminopeptidase; DE AltName: Full=Aminopeptidase P; DE Short=APP; GN Name=pepP; OrderedLocusNames=MG324; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 297-354. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: Release of any N-terminal amino acid, CC including proline, that is linked to proline, even from a CC dipeptide or tripeptide. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the peptidase M24B 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; L43967; AAC71546.1; -; Genomic_DNA. DR EMBL; U01755; AAD10569.1; -; Genomic_DNA. DR EMBL; U01717; AAC43191.1; ALT_TERM; Unassigned_DNA. DR PIR; H64235; H64235. DR RefSeq; WP_009885960.1; NZ_AAGX01000013.1. DR ProteinModelPortal; P47566; -. DR STRING; 243273.MgenG_010200003058; -. DR EnsemblBacteria; AAC71546; AAC71546; MG_324. DR KEGG; mge:MG_324; -. DR PATRIC; 20010204; VBIMycGen98045_0379. DR eggNOG; ENOG4105DC7; Bacteria. DR eggNOG; COG0006; LUCA. DR KO; K01262; -. DR OMA; QAPGEMD; -. DR OrthoDB; EOG618QTW; -. DR BioCyc; MGEN243273:GH2R-372-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; 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 3: Inferred from homology; KW Aminopeptidase; Complete proteome; Hydrolase; Manganese; KW Metal-binding; Metalloprotease; Protease; Reference proteome. FT CHAIN 1 354 Putative Xaa-Pro aminopeptidase. FT /FTId=PRO_0000185077. FT METAL 213 213 Manganese 2. {ECO:0000250}. FT METAL 224 224 Manganese 1. {ECO:0000250}. FT METAL 224 224 Manganese 2. {ECO:0000250}. FT METAL 290 290 Manganese 1. {ECO:0000250}. FT METAL 319 319 Manganese 1. {ECO:0000250}. FT METAL 333 333 Manganese 1. {ECO:0000250}. FT METAL 333 333 Manganese 2. {ECO:0000250}. SQ SEQUENCE 354 AA; 39815 MW; 8B259F2DE99501D0 CRC64; MISELQQKIT VLKDLLKTNK ADAILIGSDQ NRFWLTNFPS SAGWLIITSN KAKLFIDGRY YEAARNFINP IVEVELFVSF KQVKAFCESN GINHLLIEGD YLTFNYQDWI QAICKQYTVI NAQEIRRVKL PSEIQAIEKA VDITRKVAVK LKRFIKPKMT ELFISQWITN ELVKQGGAKN SFDPIVATGK NGANPHHKPT KTIVKEGDFI TCDFGTIYNG YCSDITRTFL VGKKPKSAKL LSAYKKVEEA NLAGINAVNT TLTGSQVDKV CRDIIENSEF KDFFVHSTGH GVGIDIHEMP NVSQSYNKLL CENGVVTIEP GIYIPNLGGI RIEDMVLVKK EKSVWLSKSI PRAF // ID ADP1_MYCGE Reviewed; 1444 AA. AC P20796; Q49286; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=Adhesin P1; DE AltName: Full=Attachment protein; DE AltName: Full=Cytadhesin P1; DE AltName: Full=MgPa; DE Flags: Precursor; GN Name=mgpA; OrderedLocusNames=MG191; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=2925238; RA Dallo S.F., Chavoya A., Su C.-J., Baseman J.B.; RT "DNA and protein sequence homologies between the adhesins of RT Mycoplasma genitalium and Mycoplasma pneumoniae."; RL Infect. Immun. 57:1059-1065(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=2583522; DOI=10.1016/0378-1119(89)90051-6; RA Inamine J.M., Loechel S., Collier A.M., Barile M.F., Hu P.-C.; RT "Nucleotide sequence of the MgPa (mgp) operon of Mycoplasma genitalium RT and comparison to the P1 (mpp) operon of Mycoplasma pneumoniae."; RL Gene 82:259-267(1989). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-177. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 468-588; 627-723; 980-1162 AND RP 1235-1289. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: The protein is the major adhesin mediating the CC attachment of this mycoplasma to the ciliated epithelium. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC type I membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the adhesin P1 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; M31431; AAA25420.1; -; Genomic_DNA. DR EMBL; L43967; AAC71410.1; -; Genomic_DNA. DR EMBL; X61522; CAA43734.1; -; Genomic_DNA. DR EMBL; U02209; AAD12501.1; -; Genomic_DNA. DR EMBL; U01694; AAB01007.1; -; Genomic_DNA. DR EMBL; U01779; AAD10599.1; -; Genomic_DNA. DR EMBL; U02159; AAD12441.1; -; Genomic_DNA. DR PIR; A30588; A30588. DR RefSeq; WP_010869366.1; NC_000908.2. DR STRING; 243273.MgenG_010200003393; -. DR EnsemblBacteria; AAC71410; AAC71410; MG_191. DR KEGG; mge:MG_191; -. DR PATRIC; 20009826; VBIMycGen98045_0219. DR OMA; GKENEFA; -. DR OrthoDB; EOG6DVJMM; -. DR BioCyc; MGEN243273:GH2R-200-MONOMER; -. DR Proteomes; UP000000807; 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:0020035; P:cytoadherence to microvasculature, mediated by symbiont protein; IEA:UniProtKB-KW. DR InterPro; IPR022400; Adhesin_P1. DR InterPro; IPR004940; Adhesin_P1_dom. DR InterPro; IPR022116; CytadhesinP1. DR Pfam; PF03257; Adhesin_P1; 1. DR Pfam; PF12378; CytadhesinP1; 2. DR TIGRFAMs; TIGR03839; termin_org_P1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Cytadherence; Membrane; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 30 {ECO:0000255}. FT CHAIN 31 1444 Adhesin P1. FT /FTId=PRO_0000020628. FT TRANSMEM 1353 1373 Helical. {ECO:0000255}. FT CONFLICT 1160 1161 SQ -> FA (in Ref. 5). {ECO:0000305}. SQ SEQUENCE 1444 AA; 159651 MW; DB1DFF7A90FFF58A CRC64; MHQPKKRLAK KSWAFLTAAL TLGVITGVGG YFLFNQNKQR SSVSNFAYQP KQLSVKHQQA VDETLTPWTW NNNNFSSLKI TGENPGSFGL VRSQNDNLNI SSVTKNSSDD NLKYLNAVEK YLDGQQNFAI RRYDNNGRAL YDINLAKMEN PSTVQRGLNG EPIFDPFKGF GLTGNAPTDW NEIKGKVPVE VVQSPHSPNL YFVLLVPKVA LEYHNLNNQV VKESLEVKAT QSSFNPTQRL QKDSPVKDSS KQGEKLSETT ASSMSSGMAT STRAKALKVE VERGSQSDSL LKNDFAKKPL KHKNSSGEVK LEAEKEFTEA WKPLLTTDQI AREKGMGATV VSFYDAPYSE NHTAFGLVDH IDPKKMVENY PPSWKTPKWN HHGIWDYNAR NLLLQTTGFF NPRRHPEWFD EGQAKADNTS PGFKVGDTDH KKDGFKKNSS SPIALPFEAY FANIGNMVAI GNSVFIFGGN GHATKMFTTN PLSIGVFRIK YTDNFSKSSV TGWPYAVLFG GLINPQTNGL KDLPLGTNRW FEYVPRMAVS GVKWVGNQLV LAGTLTMGDT ATVPRLKYDQ LEKHLNLVAQ GQGLLREDLQ IFTPYGWANR PDIPVGAWLQ DEMGSKFGPH YFLNNPDIQD NVNNDTVEAL ISSYKNTDKL KHVYPYRYSG LYAWQLFNWS NKLTNTPLSA NFVNENSYAP NSLFAAILNE DLLTGLSDKI FYGKENEFAE NEADRFNQLL SLNPNPNTNW ARYLNVVQRF TTGPNLDSST FDQFLDFLPW IGNGKPFSNS PSPSTSASSS TPLPTFSNIN VGVKSMITQH LNKENTRWVF IPNFSPDIWT GAGYRVQSAN QKNGIPFEQV KPSNNSTPFD PNSDDNKVTP SGGSSKPTTY PALPNSISPT SDWINALTFT NKNNPQRNQL LLRSLLGTIP VLINKSGDSN DQFNKDSEQK WDKTETNEGN LPGFGEVNGL YNAALLHTYG FFGTNTNSTD PKIGFKADSS SSSSSTLVGS GLNWTSQDVG NLVVINDTSF GFQLGGWFIT FTDFIRPRTG YLGITLSSLQ DQTIIWADQP WTSFKGSYLD SDGTPKSLWD PTALKSLPNS STTYDTNPTL SPSFQLYQPN KVKAYQTTNT YNKLIEPVDA TSAATNMTSL LKLLTTKNIK AKLGKGTASS QGNNNGGGVS QTINTITTTG NISEGLKEET SIQAETLKKF FDSKQNNKSE IGIGDSTFTK MDGKLTGVVS TPLVNLINGQ GATSDSDTEK ISFKPGNQID FNRLFTLPVT ELFDPNTMFV YDQYVPLLVN LPSGFDQASI RLKVISYSVE NQTLGVRLEF KDPQTQQFIP VLNASSTGPQ TVFQPFNQWA DYVLPLIVTV PIVVIILSVT LGLTIGIPMH RNKKALQAGF DLSNKKVDVL TKAVGSVFKE IINRTGISNA PKKLKQATPT KPTPKTPPKP PVKQ // ID AMPA_MYCGE Reviewed; 447 AA. AC P47631; Q49371; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Probable cytosol aminopeptidase; DE EC=3.4.11.1; DE AltName: Full=Leucine aminopeptidase; DE Short=LAP; DE EC=3.4.11.10; DE AltName: Full=Leucyl aminopeptidase; GN Name=pepA; OrderedLocusNames=MG391; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 AND 138-245. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Presumably involved in the processing and regular CC turnover of intracellular proteins. Catalyzes the removal of CC unsubstituted N-terminal amino acids from various peptides (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|- CC Yaa-, in which Xaa is preferably Leu, but may be other amino acids CC including Pro although not Arg or Lys, and Yaa may be Pro. Amino CC acid amides and methyl esters are also readily hydrolyzed, but CC rates on arylamides are exceedingly low. CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, CC preferentially leucine, but not glutamic or aspartic acids. 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 peptidase M17 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD12535.1; 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; L43967; AAC71619.1; -; Genomic_DNA. DR EMBL; U02268; AAD12535.1; ALT_INIT; Genomic_DNA. DR EMBL; U01801; AAD12327.1; -; Genomic_DNA. DR EMBL; U01802; AAD12328.1; -; Genomic_DNA. DR PIR; C64243; C64243. DR RefSeq; WP_009885632.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47631; -. DR STRING; 243273.MgenG_010200000555; -. DR EnsemblBacteria; AAC71619; AAC71619; MG_391. DR KEGG; mge:MG_391; -. DR PATRIC; 20010368; VBIMycGen98045_0457. DR eggNOG; ENOG4105BZ6; Bacteria. DR eggNOG; COG0260; LUCA. DR KO; K01255; -. DR OMA; HHPANAR; -. DR OrthoDB; EOG6FV8B3; -. DR BioCyc; MGEN243273:GH2R-448-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1. DR InterPro; IPR011356; Leucine_aapep/pepB. DR InterPro; IPR000819; Peptidase_M17_C. DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept. DR Pfam; PF00883; Peptidase_M17; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR PROSITE; PS00631; CYTOSOL_AP; 1. PE 3: Inferred from homology; KW Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Manganese; KW Metal-binding; Protease; Reference proteome. FT CHAIN 1 447 Probable cytosol aminopeptidase. FT /FTId=PRO_0000165766. FT ACT_SITE 230 230 {ECO:0000255}. FT ACT_SITE 304 304 {ECO:0000255}. FT METAL 218 218 Manganese 2. {ECO:0000250}. FT METAL 223 223 Manganese 1. {ECO:0000250}. FT METAL 223 223 Manganese 2. {ECO:0000250}. FT METAL 241 241 Manganese 2. {ECO:0000250}. FT METAL 300 300 Manganese 1. {ECO:0000250}. FT METAL 302 302 Manganese 1. {ECO:0000250}. FT METAL 302 302 Manganese 2. {ECO:0000250}. SQ SEQUENCE 447 AA; 49107 MW; 2AFCABC9C10477E3 CRC64; MRINKPFSDD SNTVVFVSSK TYGVKEEAAH NPNVEFGVVL PTDFPAFNRA LVQFLKRKKT KLNINLDSLI ELYKKNENSG CFHTAIKTVI TSVTFCETTP FTMKTKPEKN VEVAVQCAVE YHNLVKEYET VGEYVNLARE LQDTPSDLLY SEVFVKHFEK AASKLPVKIK VLKQSDLIKK KMGLLLGVNQ GSEREARLLV ISYQANKNSK EKLAFVGKGI TYDSGGMNIK TGDYMRGMKY DMSGAAIVCS TVLALAKNKV KTNVVAVAAL TENLPGAKAQ RPDDIKIAYN GKSVEIDNTD AEGRLVLADA ITYAAKDLAA THIIDVATLT GLMSYILSTT YTGIFSTCDH QWESFKKAAC SAGEPVWRLP MHPDYLKPLQ LTKLADLQNS TSARGAGSSR AACFLAEFRE GVSLIHCDIA STASIENLGQ GVLVRTLYER ASQLANK // ID APT_MYCGE Reviewed; 180 AA. AC P47518; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 102. 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=MG276; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-180. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71498.1; -; Genomic_DNA. DR EMBL; U01786; AAD10608.1; -; Genomic_DNA. DR PIR; E64230; E64230. DR RefSeq; WP_010869402.1; NZ_AAGX01000009.1. DR ProteinModelPortal; P47518; -. DR STRING; 243273.MgenG_010200002664; -. DR EnsemblBacteria; AAC71498; AAC71498; MG_276. DR KEGG; mge:MG_276; -. DR PATRIC; 20010052; VBIMycGen98045_0318. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; MGEN243273:GH2R-305-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000807; 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 1 180 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149411. SQ SEQUENCE 180 AA; 19976 MW; 81E63CDB8DF1F234 CRC64; MDQNFKLLDQ AIKRFENFPN QGTLFYDITP VFSNPQLFNF VLTQMAQFIK AINAEAIVCP EARGFIFGGA LASKTQLPLV LVRKANKLPG QLISASYDLE YRKHAVLEMS TTSLIQANNA KRCVIVDDVL ATAGTVAAID QLLKQLNGET VGYCFLIELK KLNGKAKLQP NVVSKILLHY // ID ATCL_MYCGE Reviewed; 874 AA. AC P47317; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 117. DE RecName: Full=Probable cation-transporting P-type ATPase; DE EC=3.6.3.-; GN Name=pacL; OrderedLocusNames=MG071; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 404-490. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). CC -!- FUNCTION: Could mediate calcium influx. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) CC (TC 3.A.3) family. Type II 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; L43967; AAC71289.1; -; Genomic_DNA. DR EMBL; X61532; CAA43744.1; -; Genomic_DNA. DR PIR; H64207; H64207. DR RefSeq; WP_009885927.1; NZ_AAGX01000011.1. DR ProteinModelPortal; P47317; -. DR STRING; 243273.MgenG_010200002846; -. DR EnsemblBacteria; AAC71289; AAC71289; MG_071. DR KEGG; mge:MG_071; -. DR PATRIC; 20009544; VBIMycGen98045_0081. DR eggNOG; ENOG4105C52; Bacteria. DR eggNOG; COG0474; LUCA. DR KO; K01537; -. DR OMA; DIAFDNN; -. DR OrthoDB; EOG6HF5WH; -. DR BioCyc; MGEN243273:GH2R-74-MONOMER; -. DR Proteomes; UP000000807; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.20.1110.10; -; 2. DR Gene3D; 2.70.150.10; -; 2. DR Gene3D; 3.40.1110.10; -; 1. DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C. DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N. DR InterPro; IPR023299; ATPase_P-typ_cyto_domN. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR023298; ATPase_P-typ_TM_dom. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR001757; P_typ_ATPase. DR Pfam; PF00689; Cation_ATPase_C; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR PRINTS; PR00120; HATPASE. DR SMART; SM00831; Cation_ATPase_N; 1. DR SUPFAM; SSF56784; SSF56784; 2. DR TIGRFAMs; TIGR01494; ATPase_P-type; 4. DR PROSITE; PS00154; ATPASE_E1_E2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Magnesium; KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 874 Probable cation-transporting P-type FT ATPase. FT /FTId=PRO_0000046162. FT TOPO_DOM 1 41 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TOPO_DOM 63 79 Extracellular. {ECO:0000255}. FT TRANSMEM 80 100 Helical. {ECO:0000255}. FT TOPO_DOM 101 237 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 238 257 Helical. {ECO:0000255}. FT TOPO_DOM 258 275 Extracellular. {ECO:0000255}. FT TRANSMEM 276 293 Helical. {ECO:0000255}. FT TOPO_DOM 294 644 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 645 664 Helical. {ECO:0000255}. FT TOPO_DOM 665 687 Extracellular. {ECO:0000255}. FT TRANSMEM 688 708 Helical. {ECO:0000255}. FT TOPO_DOM 709 726 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 727 749 Helical. {ECO:0000255}. FT TOPO_DOM 750 770 Extracellular. {ECO:0000255}. FT TRANSMEM 771 790 Helical. {ECO:0000255}. FT TOPO_DOM 791 803 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 804 826 Helical. {ECO:0000255}. FT TOPO_DOM 827 844 Extracellular. {ECO:0000255}. FT TRANSMEM 845 865 Helical. {ECO:0000255}. FT TOPO_DOM 866 874 Cytoplasmic. {ECO:0000255}. FT ACT_SITE 331 331 4-aspartylphosphate intermediate. FT {ECO:0000250}. FT METAL 589 589 Magnesium. {ECO:0000250}. FT METAL 593 593 Magnesium. {ECO:0000250}. SQ SEQUENCE 874 AA; 96318 MW; EEFAADA0BD4DBF7D CRC64; MNSWTGLSEQ AAIKSRQEHG ANFLPEKKAT PFWLLFLQQF KSLVVILLLL ASLLSFVVAI VSGLRSNWNF NHDLIIEWVQ PFIILLTVFA NSLIGSIQEF KAQKSASALK SLTKSFTRVF RNGELISINV SEVVVGDIIF VDAGDIIPAD GKLLQVNNLR CLESFLTGES TPVDKTIDSN EKATILEQTN LVFSGAQVVY GSGVFQVEAV GIKTQVGKIA KTVDDSVTKL SPLQQKLEKI GKWFSWFGLG LFAVVFLVQT ALLGFDNFTN NWSIALIGAI ALVVAIIPEG LVTFINVIFA LSVQKLTKQK AIIKYLSVIE TLGSVQIICT DKTGTLTQNQ MKVVDHFCFN STTQTDLARA LCLCNNASIS KDANKTGDPT EIALLEWKDR SQLDLKTYYR VYEKAFDSIR KLMTVVVQKD NRFIVIVKGA PDVLLPLCNN VQNEVKNIEN LLDQSAGQGL RTLAVALKVL YKFDQNDQKQ IDELENNLEF LGFVSLQDPP RKESKEAILA CKKANITPIM ITGDHLKTAT VIAKELGILT LDNQAVLGSE LDEKKILDYR VFARVTPQQK LAIVSAWKEA GFTVSVTGDG VNDAPALIKS DVGCCMGITG VDIAKDASDL IISDDNFATI VNGIEEGRKT FLTCKRVLLN LFLTSIAGTV VVLLGLFILG QVFKTNLLQQ GHDFQVFSPT QLLIINLFVH GFPAVALAVQ PVKEKLMVGS FSTKNLFYNR QGFDLIWQSL FLSFLTLLFY SLGIIYAINN RDLQTSGDLI NRAGSTCGFF ILGASAALNS LNLMVDKPLL MTNPWFFKLV WIGSLASILV FLLIIFINPL GLVFNVLQDL TNHPVLISYS FGGVILYMGM NEVVKLIRLG YGNI // ID ATPF_MYCGE Reviewed; 208 AA. AC P47643; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 107. 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}; DE Flags: Precursor; GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; OrderedLocusNames=MG403; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 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; L43967; AAC71631.1; -; Genomic_DNA. DR PIR; F64244; F64244. DR RefSeq; WP_009885620.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47643; -. DR STRING; 243273.MgenG_010200000475; -. DR EnsemblBacteria; AAC71631; AAC71631; MG_403. DR KEGG; mge:MG_403; -. DR PATRIC; 20010394; VBIMycGen98045_0470. DR eggNOG; ENOG4106CUG; Bacteria. DR eggNOG; COG0711; LUCA. DR KO; K02109; -. DR OMA; SINQKTH; -. DR OrthoDB; EOG63VC12; -. DR BioCyc; MGEN243273:GH2R-460-MONOMER; -. DR Proteomes; UP000000807; 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 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. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell membrane; CF(0); Complete proteome; KW Hydrogen ion transport; Ion transport; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Transport. FT SIGNAL 1 27 {ECO:0000250}. FT CHAIN 28 208 ATP synthase subunit b. FT /FTId=PRO_0000002631. FT TRANSMEM 49 69 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01398}. FT LIPID 28 28 N-palmitoyl cysteine. {ECO:0000250}. FT LIPID 28 28 S-diacylglycerol cysteine. {ECO:0000250}. SQ SEQUENCE 208 AA; 24603 MW; 0AB6526A367F84E6 CRC64; MVKAKKLVFK WSLLVFSFFT LSLFLVSCTE NVREIKSSSV INELFPNFWV FITHLLAFFI LLTLMIFLFW KPTQRFLNNR KNLLEAQIKQ ANELEKQARN LLEESNQRHE KALIVSKEIV DQANYEALQL KSEIEKTANR QANLMIFQAR QEIEKERRSL KEQSIKESVE LAMLAAQELI LKKIDQKSDR EFIDKFIRDL EANETEDD // ID ATPB_MYCGE Reviewed; 476 AA. AC P47639; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-MAY-2016, entry version 119. 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}; OrderedLocusNames=MG399; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-378. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 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; L43967; AAC71627.1; -; Genomic_DNA. DR EMBL; U01752; AAD10566.1; -; Genomic_DNA. DR ProteinModelPortal; P47639; -. DR SMR; P47639; 10-468. DR PRIDE; P47639; -. DR EnsemblBacteria; AAC71627; AAC71627; MG_399. DR KEGG; mge:MG_399; -. DR PATRIC; 20010386; VBIMycGen98045_0466. DR KO; K02112; -. DR OMA; FKESGVI; -. DR OrthoDB; EOG6HQSP3; -. DR BioCyc; MGEN243273:GH2R-456-MONOMER; -. DR Proteomes; UP000000807; 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 membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Hydrolase; Ion transport; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 476 ATP synthase subunit beta. FT /FTId=PRO_0000144451. FT NP_BIND 157 164 ATP. {ECO:0000255|HAMAP-Rule:MF_01347}. SQ SEQUENCE 476 AA; 52549 MW; 00E69866B188CE42 CRC64; MIKKENLTYG KVHQVIGPVV DVIFSESKQL PRVYDCLSVQ LKKSELFLEA TQLIGDDIVR CIALGPTEGL ARNVKVTNYN HPIEVPVGKN VLGRMFNVLG EPIDGKEPLP KKPKLSIHRN PPAFDEQPNT VDIFETGIKV IDLLTPYVRG GKIGLFGGAG VGKTVLVQEL IHNIAKEHSG LSVFAGVGER TREGNDLYYE MIQGGVIDKT VLVFGQMNEP PGARMRVALT ALTMAEYFRD HDNQNVLLFI DNIFRFTQAG SEVSALLGRM PSAVGYQPTL AIEMGKLQER IASTKTGSIT SVQAIYVPAD DLTDPAPATT FTHLDAKTVL DRNIAALGIF PAINPLESTS RLLDPSVVGI NHYKVALGVQ NILQRFAELQ DIIAILGIDE LSDEDKIIVE RARRIRNFLS QPFFVAEKFS GIAGKYVSLN DTVQSFKEIL EGKHDHLPEQ AFFYVGTIQE AVEKAKRLNQ EFDKTK // ID ATP6_MYCGE Reviewed; 292 AA. AC P47645; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393}; DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393}; DE AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393}; GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; OrderedLocusNames=MG405; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Key component of the proton channel; it plays a direct CC role in the translocation of protons across the membrane. CC {ECO:0000255|HAMAP-Rule:MF_01393}. 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_01393}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01393}. CC -!- SIMILARITY: Belongs to the ATPase A chain family. CC {ECO:0000255|HAMAP-Rule:MF_01393}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71633.1; -; Genomic_DNA. DR PIR; H64244; H64244. DR RefSeq; WP_009885618.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47645; -. DR STRING; 243273.MgenG_010200000465; -. DR EnsemblBacteria; AAC71633; AAC71633; MG_405. DR KEGG; mge:MG_405; -. DR PATRIC; 20010400; VBIMycGen98045_0473. DR eggNOG; ENOG4105W11; Bacteria. DR eggNOG; COG0356; LUCA. DR KO; K02108; -. DR OMA; WNQPQLF; -. DR OrthoDB; EOG68DD2G; -. DR BioCyc; MGEN243273:GH2R-462-MONOMER; -. DR Proteomes; UP000000807; 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; 1. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR SUPFAM; SSF81336; SSF81336; 1. DR PROSITE; PS00449; ATPASE_A; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell membrane; CF(0); Complete proteome; KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 292 ATP synthase subunit a. FT /FTId=PRO_0000082060. FT TRANSMEM 39 59 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 73 93 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 102 122 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 128 148 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 172 192 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 196 216 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 231 251 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. SQ SEQUENCE 292 AA; 33176 MW; 641565799CD06CDB CRC64; MSPREIVLKE TNQIDFISNQ SIFDISPISG WKPFAPTDQI LGIFIVFVLL LTFFIFYKLK LKKADSLKNN SYFLLLFQML FVWVQDTTAD LLGEENKKFA PYFLMLLLYI VSSNLVSLLG GISPPTSSLT FTFSLGLATF IGIVVMGIRY QRWNFFKEFA FGITVKGKKY STFIPNPFSI LSGFAPLFSI SLRLWGNILA GTVILALFYN FWIFIFSSIN NQPLALSLGT VFAGLITPVL HIYFDVIAGV LQGYVFVMLT YNYWAKMRNQ GLENNNASEL HFKGIKVIQE NI // ID ATPD_MYCGE Reviewed; 176 AA. AC P47642; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=ATP synthase subunit delta; DE AltName: Full=ATP synthase F(1) sector subunit delta; DE AltName: Full=F-type ATPase subunit delta; DE Short=F-ATPase subunit delta; GN Name=atpH; OrderedLocusNames=MG402; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 (By similarity). {ECO:0000250}. 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 (By similarity). CC {ECO:0000250}. 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 (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATPase delta chain 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; L43967; AAC71630.1; -; Genomic_DNA. DR PIR; E64244; E64244. DR RefSeq; WP_009885621.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47642; -. DR STRING; 243273.MgenG_010200000480; -. DR EnsemblBacteria; AAC71630; AAC71630; MG_402. DR KEGG; mge:MG_402; -. DR PATRIC; 20010392; VBIMycGen98045_0469. DR eggNOG; ENOG4106F7A; Bacteria. DR eggNOG; COG0712; LUCA. DR KO; K02113; -. DR OMA; SAFEIDN; -. DR OrthoDB; EOG6DNTDK; -. DR BioCyc; MGEN243273:GH2R-459-MONOMER; -. DR Proteomes; UP000000807; 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:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. DR Gene3D; 1.10.520.20; -; 1. DR InterPro; IPR020781; ATPase_OSCP/d_CS. DR InterPro; IPR026015; ATPase_OSCP/delta_N. DR InterPro; IPR000711; ATPase_OSCP/dsu. DR Pfam; PF00213; OSCP; 1. DR PRINTS; PR00125; ATPASEDELTA. DR SUPFAM; SSF47928; SSF47928; 1. DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1. DR PROSITE; PS00389; ATPASE_DELTA; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transport. FT CHAIN 1 176 ATP synthase subunit delta. FT /FTId=PRO_0000193468. SQ SEQUENCE 176 AA; 20874 MW; F4AF41258B0BAA1A CRC64; MINAQAFGTA LFQLSEEQKQ VKKIYEECHF FLKLMRNFKD GSLSFLLNSY TLTKPDKIRL VDKLFKNHFC QVFVDFLKVI ILKGYFTLVE QAIKYFFDNV ESQKHIQFIK IITAFELSSK QLNKIIAIME KRFKTKVVYK TEIDRSLISG IRIESSSHLF EKNVRDELKR IMAHFI // ID ATPL_MYCGE Reviewed; 102 AA. AC P47644; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 106. 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}; OrderedLocusNames=MG404; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 membrane {ECO:0000255|HAMAP- CC Rule:MF_01396}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01396}. CC -!- MISCELLANEOUS: Dicyclohexylcarbodiimide (DCDD) binding to the CC active glutamate residue inhibits ATPase in vitro. {ECO:0000250}. 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; L43967; AAC71632.1; -; Genomic_DNA. DR PIR; G64244; G64244. DR RefSeq; WP_009885619.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47644; -. DR STRING; 243273.MgenG_010200000470; -. DR EnsemblBacteria; AAC71632; AAC71632; MG_404. DR KEGG; mge:MG_404; -. DR PATRIC; 20010398; VBIMycGen98045_0472. DR eggNOG; ENOG41082I9; Bacteria. DR eggNOG; ENOG410ZXJ4; LUCA. DR KO; K02110; -. DR OMA; CDAIARN; -. DR OrthoDB; EOG68H8G3; -. DR BioCyc; MGEN243273:GH2R-461-MONOMER; -. DR Proteomes; UP000000807; 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 membrane; CF(0); Complete proteome; KW Hydrogen ion transport; Ion transport; Lipid-binding; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 102 ATP synthase subunit c. FT /FTId=PRO_0000112152. FT TRANSMEM 34 54 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01396}. FT TRANSMEM 80 100 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01396}. FT SITE 83 83 Reversibly protonated during proton FT transport. {ECO:0000255|HAMAP- FT Rule:MF_01396}. SQ SEQUENCE 102 AA; 10602 MW; 9E7B73831C54F173 CRC64; MEHVNEILAT VGVILQQTQT TQDVNASAKL GAYIGAGVTM IAGSTVGIGQ GYIFGKAVEA IARNPEVEKQ VFKLIFIGSA VSESTAIYGL LISFILIFVA GA // ID ATPA_MYCGE Reviewed; 518 AA. AC P47641; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 124. 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}; OrderedLocusNames=MG401; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 325-518. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 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 -!- SEQUENCE CAUTION: CC Sequence=AAC43205.2; Type=Frameshift; Positions=455; 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; L43967; AAC71629.1; -; Genomic_DNA. DR EMBL; U01727; AAC43205.2; ALT_FRAME; Genomic_DNA. DR PIR; D64244; D64244. DR RefSeq; WP_009885622.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47641; -. DR SMR; P47641; 17-499. DR STRING; 243273.MgenG_010200000485; -. DR PRIDE; P47641; -. DR EnsemblBacteria; AAC71629; AAC71629; MG_401. DR KEGG; mge:MG_401; -. DR PATRIC; 20010390; VBIMycGen98045_0468. DR eggNOG; ENOG4105CDG; Bacteria. DR eggNOG; COG0056; LUCA. DR KO; K02111; -. DR OMA; PVFCIYV; -. DR OrthoDB; EOG67X1S1; -. DR BioCyc; MGEN243273:GH2R-458-MONOMER; -. DR Proteomes; UP000000807; 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; 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 SUPFAM; SSF47917; SSF47917; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00962; atpA; 1. PE 3: Inferred from homology; KW ATP synthesis; ATP-binding; Cell membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Hydrolase; Ion transport; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 518 ATP synthase subunit alpha. FT /FTId=PRO_0000144335. FT NP_BIND 169 176 ATP. {ECO:0000255|HAMAP-Rule:MF_01346}. FT SITE 362 362 Required for activity. FT {ECO:0000255|HAMAP-Rule:MF_01346}. FT CONFLICT 453 453 I -> F (in Ref. 2; AAC43205). FT {ECO:0000305}. SQ SEQUENCE 518 AA; 57216 MW; 2CBBDAF094BCDEEB CRC64; MADKLNEYVA LIKTEIKKYS KKIFNSEIGQ VISVADGIAK VSGLENALLN ELIQFENNIQ GIVLNLEQNT VGIALFGDYS SLREGSTAKR THSVMKTPVG DVMLGRIVNA LGEAIDGRGD IKATEYDQIE KIAPGVMKRK SVNQPLETGI LTIDALFPIG KGQRELIVGD RQTGKTAIAI DTIINQKDKD VYCVYVAIGQ KNSSVAQIVH QLEVNDSMKY TTVVCATASD SDSMVYLSPF TGITIAEYWL KKGKDVLIVF DDLSKHAVAY RTLSLLLKRP PGREAFPGDV FYLHSRLLER ACKLNDENGG GSITALPIIE TQAGDISAYI PTNVISITDG QLFMVSSLFN AGQRPAIQIG LSVSRVGSAA QTKAIKQQTG SLKLELAQYS ELDSFSQFGS DLDENTKKVL EHGKRVMEMI KQPNGKPYSQ VHEALFLFAI NKAFIKFIPV DEIAKFKQRI TEEFNGSHPL FKELSNKKEF TEDLESKTKT AFKMLVKRFI STLTDYDITK FGSIEELN // ID ATPE_MYCGE Reviewed; 133 AA. AC P47638; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=ATP synthase epsilon chain; DE AltName: Full=ATP synthase F1 sector epsilon subunit; DE AltName: Full=F-ATPase epsilon subunit; GN Name=atpC; OrderedLocusNames=MG398; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. {ECO:0000250}. 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 membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATPase epsilon chain 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; L43967; AAC71626.1; -; Genomic_DNA. DR PIR; A64244; A64244. DR RefSeq; WP_010869467.1; NC_000908.2. DR ProteinModelPortal; P47638; -. DR EnsemblBacteria; AAC71626; AAC71626; MG_398. DR KEGG; mge:MG_398; -. DR PATRIC; 20010384; VBIMycGen98045_0465. DR KO; K02114; -. DR OMA; CKIIFAD; -. DR OrthoDB; EOG6DRPKK; -. DR BioCyc; MGEN243273:GH2R-455-MONOMER; -. DR Proteomes; UP000000807; 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 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 Pfam; PF02823; ATP-synt_DE_N; 1. DR SUPFAM; SSF51344; SSF51344; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transport. FT CHAIN 1 133 ATP synthase epsilon chain. FT /FTId=PRO_0000188160. SQ SEQUENCE 133 AA; 15151 MW; AD19191B10102A61 CRC64; MKLLRFLVLS PSGIKLDKTI ISAQVKTTEG YIGLNFNRAP LIAAIQSHLC KIIFADQTKR EAIIGAGLML IKKTEAKIFT ENFVFADEVD INETLKRKTE LERKIHHIKD AKLNVKIEQN LMFELLKLSS KKK // ID AZOR_MYCGE Reviewed; 197 AA. AC P47575; Q49357; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 3. DT 13-APR-2016, entry version 80. DE RecName: Full=FMN-dependent NADH-azoreductase {ECO:0000255|HAMAP-Rule:MF_01216}; DE EC=1.7.-.- {ECO:0000255|HAMAP-Rule:MF_01216}; DE AltName: Full=Azo-dye reductase {ECO:0000255|HAMAP-Rule:MF_01216}; DE AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216}; GN Name=azoR {ECO:0000255|HAMAP-Rule:MF_01216}; OrderedLocusNames=MG333; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Catalyzes the reductive cleavage of azo bond in aromatic CC azo compounds to the corresponding amines. Requires NADH, but not CC NADPH, as an electron donor for its activity. {ECO:0000255|HAMAP- CC Rule:MF_01216}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01216}; CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01216}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01216}. CC -!- SIMILARITY: Belongs to the azoreductase type 1 family. CC {ECO:0000255|HAMAP-Rule:MF_01216}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD12538.1; 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; L43967; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U02249; AAD12538.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_009885986.1; NZ_AAGX01000016.1. DR ProteinModelPortal; P47575; -. DR STRING; 243273.MgenG_010200003230; -. DR eggNOG; ENOG410834W; Bacteria. DR eggNOG; COG1182; LUCA. DR OMA; IDAICIA; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008752; F:FMN reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; IEA:InterPro. DR Gene3D; 3.40.50.360; -; 1. DR HAMAP; MF_01216; Azoreductase_type1; 1. DR InterPro; IPR003680; Flavodoxin_fold. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR023048; NADH-azoreductase_FMN-depdnt. DR Pfam; PF02525; Flavodoxin_2; 1. DR SUPFAM; SSF52218; SSF52218; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1 197 FMN-dependent NADH-azoreductase. FT /FTId=PRO_0000166344. FT CONFLICT 44 47 NELP -> MNYQ (in Ref. 3; AAD12538). FT {ECO:0000305}. SQ SEQUENCE 197 AA; 22189 MW; 5CAAE33C088ABF00 CRC64; MKKVIIVDAS VTPSGSYTHL LLDRFLQTYK KQNSSVEFID WNLNELPVGK ISYNTQNASN FFSFENSDYY IDALKTAYGI VILAPMTNFN YPASLKNFID HVFVANKTFQ DKYVTKGASK GLLTNLKVVV LASQGAPLGW YPWADHVSNL KGLFGFAGVT HFESVLIDDT KILYKDKNKQ EVVDLFAHKV DQVANNF // ID ATPG_MYCGE Reviewed; 279 AA. AC P47640; Q49511; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=ATP synthase gamma chain {ECO:0000255|HAMAP-Rule:MF_00815}; DE AltName: Full=ATP synthase F1 sector gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815}; DE AltName: Full=F-ATPase gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815}; GN Name=atpG {ECO:0000255|HAMAP-Rule:MF_00815}; OrderedLocusNames=MG400; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 55-229. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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:0000255|HAMAP-Rule:MF_00815}. 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:0000255|HAMAP- CC Rule:MF_00815}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00815}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00815}. CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. CC {ECO:0000255|HAMAP-Rule:MF_00815}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71628.1; -; Genomic_DNA. DR EMBL; U01703; AAB01015.1; -; Genomic_DNA. DR PIR; C64244; C64244. DR RefSeq; WP_009885623.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47640; -. DR STRING; 243273.MgenG_010200000490; -. DR EnsemblBacteria; AAC71628; AAC71628; MG_400. DR KEGG; mge:MG_400; -. DR PATRIC; 20010388; VBIMycGen98045_0467. DR eggNOG; ENOG4105J80; Bacteria. DR eggNOG; COG0224; LUCA. DR KO; K02115; -. DR OMA; FLYTAQN; -. DR OrthoDB; EOG6R5C97; -. DR BioCyc; MGEN243273:GH2R-457-MONOMER; -. DR Proteomes; UP000000807; 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; 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. PE 3: Inferred from homology; KW ATP synthesis; Cell membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transport. FT CHAIN 1 279 ATP synthase gamma chain. FT /FTId=PRO_0000073320. FT CONFLICT 55 58 QVVV -> PSSC (in Ref. 2; AAB01015). FT {ECO:0000305}. FT CONFLICT 219 229 DVALYGGLVET -> WCGSVWWPCWN (in Ref. 2; FT AAB01015). {ECO:0000305}. SQ SEQUENCE 279 AA; 32422 MW; 1C423F328E330AD5 CRC64; MAFIQEIKRR MNTVKSTIKI TNAMKMVSRA KFIKFKKQFQ EISLFFNEFY KAVGQVVVSL KEPKKKPDNQ KTLWIMMSSS LGLCGQHNSN MNKLLKANFK ADDKIFFLGR KNQSFWNKNS QYNPAVGFID IQDRDINFDY CQTIFDQIMD AFKEFKLDRI CMVYTKFKNS LIQQSQLFQV FPFDVETFKT LNPVVTDQQL DFEPDQATII NLITPQFFDV ALYGGLVETK LCESASRQNA MEAATKNAKD LLDKYTLQFN KLRQNSITEE IIEVIGGMN // ID CDD_MYCGE Reviewed; 130 AA. AC P47298; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Cytidine deaminase; DE Short=CDA; DE EC=3.5.4.5; DE AltName: Full=Cytidine aminohydrolase; GN Name=cdd; OrderedLocusNames=MG052; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-130. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine CC and 2'-deoxycytidine for UMP synthesis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC -!- CATALYTIC ACTIVITY: 2'deoxycytidine + H(2)O = 2'-deoxyuridine + CC NH(3). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 CMP/dCMP-type deaminase domain. CC {ECO:0000255|PROSITE-ProRule:PRU01083}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71268.1; -; Genomic_DNA. DR EMBL; U02108; AAD12378.1; -; Genomic_DNA. DR PIR; G64205; G64205. DR RefSeq; WP_010869308.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47298; -. DR STRING; 243273.MgenG_010200001135; -. DR EnsemblBacteria; AAC71268; AAC71268; MG_052. DR KEGG; mge:MG_052; -. DR PATRIC; 20009484; VBIMycGen98045_0052. DR eggNOG; ENOG4107ZT6; Bacteria. DR eggNOG; COG0295; LUCA. DR KO; K01489; -. DR OMA; IISPCAG; -. DR OrthoDB; EOG6XDH25; -. DR BioCyc; MGEN243273:GH2R-52-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-EC. 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; 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 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 130 Cytidine deaminase. FT /FTId=PRO_0000171679. FT DOMAIN 3 130 CMP/dCMP-type deaminase. FT {ECO:0000255|PROSITE-ProRule:PRU01083}. FT REGION 43 45 Substrate binding. {ECO:0000250}. FT ACT_SITE 56 56 Proton donor. {ECO:0000250}. FT METAL 54 54 Zinc; catalytic. {ECO:0000250}. FT METAL 88 88 Zinc; catalytic. {ECO:0000250}. FT METAL 91 91 Zinc; catalytic. {ECO:0000250}. SQ SEQUENCE 130 AA; 14974 MW; 1DF02B1718F9495F CRC64; MKVNLEWIIK QLQMIVKRAY TPFSNFKVAC MIIANNQTFF GVNIENSSFP VTLCAERSAI ASMVTSGHRK IDYVFVYFNT KNKSNSPCGM CRQNLLEFSH QKTKLFCIDN DSSYKQFSID ELLMNGFKKS // ID CH10_MYCGE Reviewed; 110 AA. AC P47633; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=10 kDa chaperonin; DE AltName: Full=GroES protein; DE AltName: Full=Protein Cpn10; GN Name=groS; Synonyms=groES, mopB; OrderedLocusNames=MG393; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-110. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Binds to Cpn60 in the presence of Mg-ATP and suppresses CC the ATPase activity of the latter. {ECO:0000250}. CC -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GroES chaperonin 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; L43967; AAC71621.1; -; Genomic_DNA. DR EMBL; U02252; AAD12516.1; -; Genomic_DNA. DR PIR; E64243; E64243. DR RefSeq; WP_010869464.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47633; -. DR STRING; 243273.MgenG_010200000545; -. DR EnsemblBacteria; AAC71621; AAC71621; MG_393. DR KEGG; mge:MG_393; -. DR PATRIC; 20010372; VBIMycGen98045_0459. DR eggNOG; COG0234; LUCA. DR KO; K04078; -. DR OMA; MNITPIH; -. DR OrthoDB; EOG6GFGSD; -. DR BioCyc; MGEN243273:GH2R-450-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; IPR011032; GroES-like. DR Pfam; PF00166; Cpn10; 1. DR PRINTS; PR00297; CHAPERONIN10. DR SMART; SM00883; Cpn10; 1. DR SUPFAM; SSF50129; SSF50129; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 110 10 kDa chaperonin. FT /FTId=PRO_0000174789. SQ SEQUENCE 110 AA; 12029 MW; 21FAD2723A8471F5 CRC64; MNITPIHDNV LVSLVESNKE EVSKKGIITS LASNDKSDAN ANKGIVIALG AGPAYGKTEK PKYAFGVGDI IYFKEYSGIS FENEGNKYKI IGFEDVLAFE KPESGKQRKR // ID CH60_MYCGE Reviewed; 543 AA. AC P47632; Q49358; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 91. 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=MG392; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60 AND 466-543. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 -!- SEQUENCE CAUTION: CC Sequence=AAD12515.1; 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; L43967; AAC71620.1; -; Genomic_DNA. DR EMBL; U02252; AAD12515.1; ALT_INIT; Genomic_DNA. DR EMBL; U02268; AAD12534.1; -; Genomic_DNA. DR PIR; D64243; D64243. DR ProteinModelPortal; P47632; -. DR STRING; 243273.MgenG_010200000550; -. DR EnsemblBacteria; AAC71620; AAC71620; MG_392. DR KEGG; mge:MG_392; -. DR PATRIC; 20010370; VBIMycGen98045_0458. DR eggNOG; ENOG4105CJ9; Bacteria. DR eggNOG; COG0459; LUCA. DR KO; K04077; -. DR OrthoDB; EOG6JDWBZ; -. DR BioCyc; MGEN243273:GH2R-449-MONOMER; -. DR Proteomes; UP000000807; 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; -; 3. 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 1 543 60 kDa chaperonin. FT /FTId=PRO_0000063430. SQ SEQUENCE 543 AA; 58354 MW; 80FA5C7037C4BA88 CRC64; MAKELIFGKD ARTRLLQGIN KIANAVKVTV GPKGQNVILE RKFANPLITN DGVTIAKEIE LSDPVENIGA KVISVAAVST NDIAGDGTTT ATILAQEMTN RGIEIINKGA NPVNIRRGIE DASLLIIKEL EKYSKKINTN EEIEQVAAIS SGSKEIGKLI AQAMALVGKN GVITTDDAKT INTTLETTEG IEFKGTYASP YMVSDQEKME VVLEQPKILV SSLKINTIKE ILPLLEGSVE NGNPLLIVAP DFAEEVVTTL AVNKLRGTIN VVAVKCNEYG ERQKAALEDL AISSGTLAYN TEINSGFKDV TVDNLGDARK VQIAKGKTTV IGGKGNKDKI KKHVELLNGR LKQTTDKYDS DLIKERIAYL SQGVAVIRVG GATELAQKEL KLRIEDALNS TKAAVEEGII AGGGVGLLNA SCVLTNSKLK ERYENETSVE NIKEILLGFE IVQKSLEAPA RQIIQNSGVD PVKILSELKN EKTGVGFDAE TKKKVDMIAN GIIDPTKVTK TALEKAASVA SSLITTNVAV YDVKERKDNS FSE // ID CDSA_MYCGE Reviewed; 305 AA. AC Q49433; Q49309; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Putative 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=MG437; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 127-226. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC72458.1; 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; L43967; AAC72458.1; ALT_INIT; Genomic_DNA. DR EMBL; U02189; AAD12473.1; -; Genomic_DNA. DR PIR; T09771; T09771. DR STRING; 243273.MgenG_010200000280; -. DR EnsemblBacteria; AAC72458; AAC72458; MG_437. DR KEGG; mge:MG_437; -. DR PATRIC; 20010458; VBIMycGen98045_0502. DR eggNOG; ENOG4107WZU; Bacteria. DR eggNOG; COG0575; LUCA. DR KO; K00981; -. DR OrthoDB; EOG6TBHJT; -. DR BioCyc; MGEN243273:GH2R-490-MONOMER; -. DR UniPathway; UPA00557; UER00614. DR Proteomes; UP000000807; 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:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR000374; PC_trans. DR PROSITE; PS01315; CDS; 1. PE 3: Inferred from homology; KW 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 1 305 Putative phosphatidate FT cytidylyltransferase. FT /FTId=PRO_0000090739. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 152 172 Helical. {ECO:0000255}. FT TRANSMEM 212 232 Helical. {ECO:0000255}. FT TRANSMEM 264 284 Helical. {ECO:0000255}. SQ SEQUENCE 305 AA; 34196 MW; F149FA6BD9DDC080 CRC64; MIWELFTNIL KNKPKLSLSL TLLNAGIIIF GMIGTFVVVY FYKWNATVNG IWTLSFTLSV VLLWIIYIAC MSKTRIKFSL QLSYSLGAIA CFIASIGTIY FSVIRGWTTI FLLMSLAVSV DTFPFLFGKR FGKNPLIKIS PSKTWEGAFF GIISTIVVVA LLCVLYSIPF FVAKPTFNQT NGIALNTPQN YDSHNLITNI FLIAFISGGS SFYIYWWVST LALIFTGSVF AIGGDLFFSY IKRLISIKDF SKVLGKHGGV LDRFDSSSFL ISFFFVYHLI AGTISNQRLL MEPNTYFSAI TSIQS // ID CLPB_MYCGE Reviewed; 714 AA. AC P47597; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Chaperone protein ClpB; GN Name=clpB; OrderedLocusNames=MG355; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is CC involved in the recovery of the cell from heat-induced damage, in CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the CC processing of protein aggregates. Protein binding stimulates the CC ATPase activity; ATP hydrolysis unfolds the denatured protein CC aggregates, which probably helps expose new hydrophobic binding CC sites on the surface of ClpB-bound aggregates, contributing to the CC solubilization and refolding of denatured protein aggregates by CC DnaK (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The N-terminal domain probably functions as a substrate- CC discriminating domain, recruiting aggregated proteins to the ClpB CC hexamer and/or stabilizing bound proteins. The NBD2 domain is CC responsible for oligomerization, whereas the NBD1 domain CC stabilizes the hexamer probably in an ATP-dependent manner. The CC movement of the coiled-coil domain is essential for ClpB ability CC to rescue proteins from an aggregated state, probably by pulling CC apart large aggregated proteins, which are bound between the CC coiled-coils motifs of adjacent ClpB subunits in the functional CC hexamer (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ClpA/ClpB 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; L43967; AAC71580.1; -; Genomic_DNA. DR PIR; C64239; C64239. DR RefSeq; WP_010869446.1; NC_000908.2. DR ProteinModelPortal; P47597; -. DR SMR; P47597; 14-207. DR PRIDE; P47597; -. DR EnsemblBacteria; AAC71580; AAC71580; MG_355. DR KEGG; mge:MG_355; -. DR PATRIC; 20010286; VBIMycGen98045_0417. DR OMA; PVERILM; -. DR OrthoDB; EOG65F8SM; -. DR BioCyc; MGEN243273:GH2R-409-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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; 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; 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 PROSITE; PS00870; CLPAB_1; 1. DR PROSITE; PS00871; CLPAB_2; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome; Repeat; Stress response. FT CHAIN 1 714 Chaperone protein ClpB. FT /FTId=PRO_0000191141. FT NP_BIND 60 67 ATP 1. {ECO:0000250}. FT NP_BIND 466 473 ATP 2. {ECO:0000250}. FT REGION 13 196 NBD1. {ECO:0000250}. FT REGION 197 406 Linker. {ECO:0000250}. FT REGION 416 618 NBD2. {ECO:0000250}. FT REGION 619 714 C-terminal. {ECO:0000250}. FT COILED 247 385 {ECO:0000250}. SQ SEQUENCE 714 AA; 81039 MW; 53F58E85EB1D0ECD CRC64; MNINFTPAGE NRNFLQEIGR NINDEVLKNK VDPIIGRDNE IRRLIEILSR KSKNNPVLIG EPGVGKTAIV EGFVRRVVSN DVPLNLRDVE IYELSLSGLI AGTKFQGEFE KRINTILKQV KESNGRIILF IDEIHQIVGL GRNSSSGAMD IANILKPMLA RGEIKVIGAT TLKEYREYIE KDGALERRFQ KILINEPSSQ EALTIMRGLK TRWELFHNIT IFDSALVAAV EMSTRYINER NLPDKAIDLI DEAAAKIKTE MSSEPVAIDS LKREIINLET EYAALKQDKE NDNKQSKKEY LEKLKKQLDA LKQKRDSLIN EWKKEKADFE NINKLKKEIE EFQTKLETYQ SEGNYESASK ILYSDIPRLK KELESAQQKY ATSKHDLFKT EVSENEIAEV ISQTTGIPLK KLLESEKDKL LHLGDEIKKR VKGQDEAIDA VVNTVIRGRV NINDPNKPIG SFIFLGSTGV GKTELAKSLA EVLFDNEKAL IRFDMSEYME KHSVAKLIGA PPGYIGYEQS GLLTEAVRRK PYSVLLFDEI EKAHPDVTNV LLQVLDDGTL KDSQGRVVNF KNTLIIMTSN LGSNFLLEGK KDLAIQSLKK HFRPEFINRI DEIVFFNVLE KDTVLSIINS LLAQLSKRLN KQNLFFNFDS NLTEFIYKSS FDQQFGARPI KRFIDHSVAT LIAKYILQGK IKKGVGYNIA VVKDNITITQ NNKS // ID COAE_MYCGE Reviewed; 198 AA. AC P47506; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Dephospho-CoA kinase; DE EC=2.7.1.24; DE AltName: Full=Dephosphocoenzyme A kinase; GN Name=coaE; OrderedLocusNames=MG264; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71486.1; -; Genomic_DNA. DR PIR; B64229; B64229. DR RefSeq; WP_009885895.1; NZ_AAGX01000009.1. DR ProteinModelPortal; P47506; -. DR STRING; 243273.MgenG_010200002599; -. DR EnsemblBacteria; AAC71486; AAC71486; MG_264. DR KEGG; mge:MG_264; -. DR eggNOG; COG0237; LUCA. DR KO; K00859; -. DR OMA; AVMLNYW; -. DR OrthoDB; EOG6TR0JH; -. DR BioCyc; MGEN243273:GH2R-291-MONOMER; -. DR UniPathway; UPA00241; UER00356. DR Proteomes; UP000000807; 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; IEA:UniProtKB-HAMAP. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-HAMAP. 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 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 198 Dephospho-CoA kinase. FT /FTId=PRO_0000172960. FT DOMAIN 2 198 DPCK. FT NP_BIND 7 14 ATP. {ECO:0000255}. SQ SEQUENCE 198 AA; 23210 MW; 48B34E402C9B37AD CRC64; MLIAIVGKPG VGKTSLLQYL KDNYHFSVFY ADSFIHEQYQ KNNPGYQLIM DHFGKEFVNQ TEVDRKKLAN YVFSDDKLIE KLSLVTKPLL IAWIKSLKTQ FQKKLALIEI AVMLNYWNEY RSLFDYVIKL ERDDQLVNLA LQQRNSHKKV KDLIKEPNCK IDTIFNNDSI ATAALKLIKL LETFLERNKC RCDCCHIQ // ID CSD_MYCGE Reviewed; 408 AA. AC Q49420; Q49361; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Probable cysteine desulfurase; DE EC=2.8.1.7; GN Name=csd; OrderedLocusNames=MG336; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 241-330. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71561.1; -; Genomic_DNA. DR EMBL; U02256; AAD12521.1; -; Genomic_DNA. DR PIR; B64237; B64237. DR RefSeq; WP_010869440.1; NC_000908.2. DR ProteinModelPortal; Q49420; -. DR EnsemblBacteria; AAC71561; AAC71561; MG_336. DR KEGG; mge:MG_336; -. DR PATRIC; 20010232; VBIMycGen98045_0393. DR KO; K11717; -. DR OMA; HGRHDVQ; -. DR OrthoDB; EOG68DD0M; -. DR BioCyc; MGEN243273:GH2R-386-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC. 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 Pfam; PF00266; Aminotran_5; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. PE 3: Inferred from homology; KW Complete proteome; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 408 Probable cysteine desulfurase. FT /FTId=PRO_0000150299. FT MOD_RES 225 225 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 408 AA; 46618 MW; F16A009B463EBDAD CRC64; MSAIKFNPSS FRKNFKWFEN NKNWINFDNA ATSIALDVVA EASKEYYQYF CVNPHNKNPE INQKLIAIIE ETRDLLAKFF NAKKNEIIFT SSATESLNLF AFGLSSLVKS NDEIILKEDE HAANVFPWVN LAKENKAKLK IIKKTPNKSW TDAFLKACTP STKLLVITAT SNLFGNSIDY EKISKHLKKI SPNSFIVVDA VQAVPHHKID ITSANIDFLT FSTHKFYGPT GLGIAFIKSE LQSRLKPFKL GGDIFKSLDN NFKIIFKEGP SKFEAGTLNI MAIYALNKQL KFMQKEFNFS EMVFYSKQLK NLAYQLLSQN PNIVLANHDQ DVPIFAFKHK YINSADLATF LNIKKIIVRQ GSICVGKFKN KESFLRVSLL HYNTKEELLY LEKLLKTSKN SIINELIY // ID DACB_MYCGE Reviewed; 200 AA. AC P47351; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Diadenylate cyclase {ECO:0000255|HAMAP-Rule:MF_00838}; DE Short=DAC {ECO:0000255|HAMAP-Rule:MF_00838}; DE EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_00838}; DE AltName: Full=Cyclic-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00838}; DE Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00838}; GN Name=dacB {ECO:0000255|HAMAP-Rule:MF_00838}; OrderedLocusNames=MG105; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Catalyzes the condensation of 2 ATP molecules into CC cyclic di-AMP (c-di-AMP), a second messenger used to regulate CC differing processes in different bacteria. {ECO:0000255|HAMAP- CC Rule:MF_00838}. CC -!- CATALYTIC ACTIVITY: 2 ATP = 2 diphosphate + cyclic di-3',5'- CC adenylate. {ECO:0000255|HAMAP-Rule:MF_00838}. CC -!- SUBUNIT: Probably oligomerizes. {ECO:0000255|HAMAP-Rule:MF_00838}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00838}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00838}. CC -!- SIMILARITY: Belongs to the adenylate cyclase family. DacB/CdaS CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00838}. CC -!- SIMILARITY: Contains 1 DAC domain. {ECO:0000255|HAMAP- CC Rule:MF_00838}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71323.1; -; Genomic_DNA. DR PIR; F64211; F64211. DR ProteinModelPortal; P47351; -. DR STRING; 243273.MgenG_010200000770; -. DR EnsemblBacteria; AAC71323; AAC71323; MG_105. DR KEGG; mge:MG_105; -. DR PATRIC; 20009614; VBIMycGen98045_0116. DR eggNOG; ENOG4105C8B; Bacteria. DR eggNOG; COG1624; LUCA. DR OrthoDB; EOG6DRPM4; -. DR BioCyc; MGEN243273:GH2R-109-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR HAMAP; MF_00838; DacB; 1. DR InterPro; IPR014046; c-di-AMP_synthase-like. DR InterPro; IPR003390; DNA_integrity_scan_DisA_N. DR Pfam; PF02457; DisA_N; 1. DR PIRSF; PIRSF004793; UCP004793; 1. DR TIGRFAMs; TIGR00159; TIGR00159; 1. DR PROSITE; PS51794; DAC; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 200 Diadenylate cyclase. FT /FTId=PRO_0000210417. FT TRANSMEM 5 25 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00838}. FT DOMAIN 28 185 DAC. {ECO:0000255|HAMAP-Rule:MF_00838}. SQ SEQUENCE 200 AA; 22668 MW; 58142F59627063D6 CRC64; MVVNILLFIT LIFLLLLFVF LIAFAFLNKR VRNYVVRTWT SVFSKSKQNL DKKNFFDNLT STLLRLSVDK IGAIIAIEKR DSLEPYINIG YRVSSDFSPE LLVTIFYNKS SPLHDGAVIV RDYKIISVSS YFPMTRQLID VSYGSRHRSA LGLSEKSDAV VFIVSETTGK ISVALKGVIK TLSSNSDRLQ DEIIHYLSSK // ID DEOD_MYCGE Reviewed; 238 AA. AC P47295; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 92. DE RecName: Full=Purine nucleoside phosphorylase DeoD-type; DE Short=PNP; DE EC=2.4.2.1; GN Name=deoD; OrderedLocusNames=MG049; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine + CC alpha-D-ribose 1-phosphate. CC -!- CATALYTIC ACTIVITY: Purine deoxynucleoside + phosphate = purine + CC 2'-deoxy-alpha-D-ribose 1-phosphate. CC -!- SUBUNIT: Homohexamer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC71265.1; 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; L43967; AAC71265.1; ALT_INIT; Genomic_DNA. DR PIR; D64205; D64205. DR RefSeq; WP_009885712.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47295; -. DR STRING; 243273.MgenG_010200001115; -. DR EnsemblBacteria; AAC71265; AAC71265; MG_049. DR KEGG; mge:MG_049; -. DR PATRIC; 20009478; VBIMycGen98045_0049. DR eggNOG; ENOG4107TH2; Bacteria. DR eggNOG; COG0813; LUCA. DR KO; K03784; -. DR OMA; ELTICST; -. DR OrthoDB; EOG6BKJC5; -. DR BioCyc; MGEN243273:GH2R-49-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1580; -; 1. DR HAMAP; MF_01627; Pur_nucleosid_phosp; 1. DR InterPro; IPR004402; DeoD-type. DR InterPro; IPR018017; Nucleoside_phosphorylase. DR InterPro; IPR018016; Nucleoside_phosphorylase_CS. 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; TIGR00107; deoD; 1. DR PROSITE; PS01232; PNP_UDP_1; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 238 Purine nucleoside phosphorylase DeoD- FT type. FT /FTId=PRO_0000063146. FT REGION 87 90 Phosphate binding. FT {ECO:0000250|UniProtKB:P50389}. FT REGION 181 183 Purine nucleoside binding. FT {ECO:0000250|UniProtKB:P50389}. FT REGION 205 206 Purine nucleoside binding. FT {ECO:0000250|UniProtKB:P50389}. FT BINDING 4 4 Purine nucleoside; shared with dimeric FT partner. {ECO:0000250|UniProtKB:P50389}. FT BINDING 20 20 Phosphate; via amide nitrogen. FT {ECO:0000250|UniProtKB:P50389}. FT BINDING 24 24 Phosphate. FT {ECO:0000250|UniProtKB:P50389}. FT BINDING 43 43 Phosphate; shared with dimeric partner. FT {ECO:0000250|UniProtKB:P50389}. SQ SEQUENCE 238 AA; 26509 MW; C3B3523FEBBB806A CRC64; MTPHISAKKD DISKVVLMPG DPLRAKWIAE QFLDQAKLVN EVRGMFAYTG QYKSKTVTVM GHGMGIPSIG IYSYELMNFY EVETIIRIGS CGALAPQLKL KDLVIASKAW SESIYAKDMG VEIPEDKILF ATSSLVELAK ETAIKNKLDF HEGLVFCEDA FYQTRKDVIS LAKEKNSLAV EMEAHALYAN AILLKKKALT LLTVSDSLVT HEALSSELRQ KSFKQMALLA LEMTQKLI // ID DEF_MYCGE Reviewed; 216 AA. AC P47352; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 100. DE RecName: Full=Peptide deformylase; DE Short=PDF; DE EC=3.5.1.88; DE AltName: Full=Polypeptide deformylase; GN Name=def; OrderedLocusNames=MG106; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC71324.1; 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; L43967; AAC71324.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; P47352; -. DR STRING; 243273.MgenG_010200000775; -. DR EnsemblBacteria; AAC71324; AAC71324; MG_106. DR KEGG; mge:MG_106; -. DR PATRIC; 20009616; VBIMycGen98045_0117. DR eggNOG; ENOG4107YB9; Bacteria. DR eggNOG; COG0242; LUCA. DR KO; K01462; -. DR OMA; SQDPKIA; -. DR OrthoDB; EOG6PZXGQ; -. DR BioCyc; MGEN243273:GH2R-110-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0042586; F:peptide deformylase activity; IEA:UniProtKB-HAMAP. 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 3: Inferred from homology; KW Complete proteome; Hydrolase; Iron; Metal-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 216 Peptide deformylase. FT /FTId=PRO_0000082801. FT ACT_SITE 179 179 {ECO:0000250}. FT METAL 134 134 Iron. {ECO:0000250}. FT METAL 178 178 Iron. {ECO:0000250}. FT METAL 182 182 Iron. {ECO:0000250}. SQ SEQUENCE 216 AA; 25171 MW; 52D22E8FA58BEFC5 CRC64; MTKILPWLFT SIVRIILTLL FLSMTFQPTK TWLVFDDNAL INKPTEAVNF PIDEQIETCI KKMIAYVDAS YDGKAQEYDI IPGIGIAANQ IGYWKQLFYI HLNDLNKEKK CLLINPKIID QSENKAFLES GEGCLSVKKQ HKGYVIRSEW ITIKGYDWFE KKEITIKATG LFGMCLQHEF DHLQGRFFYQ RINPLNPWFK KPEWKVINPT LKTSNG // ID DEOC_MYCGE Reviewed; 223 AA. AC P47296; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 112. 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=MG050; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71266.1; -; Genomic_DNA. DR PIR; E64205; E64205. DR RefSeq; WP_010869307.1; NC_000908.2. DR ProteinModelPortal; P47296; -. DR EnsemblBacteria; AAC71266; AAC71266; MG_050. DR KEGG; mge:MG_050; -. DR PATRIC; 20009480; VBIMycGen98045_0050. DR KO; K01619; -. DR OMA; KGRIDIK; -. DR OrthoDB; EOG6QZMW5; -. DR BioCyc; MGEN243273:GH2R-50-MONOMER; -. DR UniPathway; UPA00002; UER00468. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lyase; Reference proteome; Schiff base. FT CHAIN 1 223 Deoxyribose-phosphate aldolase. FT /FTId=PRO_0000057241. FT ACT_SITE 152 152 Schiff-base intermediate with FT acetaldehyde. {ECO:0000250}. FT ACT_SITE 181 181 {ECO:0000250}. SQ SEQUENCE 223 AA; 24675 MW; 332430231CE99DB0 CRC64; MKLEYNRIID STLVKADTLP HEIDTLCADA HKYQFFAVCV NPSYVSYAKN ILKNTAVQLC CVVGFPLGQT TQKQKVYEAK IAIKEGADEI DMVMNIAEFK KRCACVITEI RAVKKVCGKR KLKVIIETAL LTNDEIKDAV NVCIDGNADY VKTSTGFSFR GASLEDVQIM NNAAANLIKI KASGGIKTAK QFIDLFQAGA SRIGTSNAVQ IMQELKKMNH EYH // ID DLDH_MYCGE Reviewed; 457 AA. AC P47513; Q49233; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 120. DE RecName: Full=Dihydrolipoyl dehydrogenase; DE EC=1.8.1.4; DE AltName: Full=Dihydrolipoamide dehydrogenase; DE AltName: Full=E3 component of pyruvate complex; GN Name=pdhD; OrderedLocusNames=MG271; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 306-404. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha- CC ketoacid dehydrogenase complexes. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = CC protein N(6)-(lipoyl)lysine + NADH. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC Note=Binds 1 FAD per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase 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; L43967; AAC71493.1; -; Genomic_DNA. DR EMBL; U01784; AAD10605.1; -; Genomic_DNA. DR PIR; I64229; I64229. DR RefSeq; WP_009885903.1; NZ_AAGX01000009.1. DR ProteinModelPortal; P47513; -. DR STRING; 243273.MgenG_010200002639; -. DR EnsemblBacteria; AAC71493; AAC71493; MG_271. DR KEGG; mge:MG_271; -. DR PATRIC; 20010042; VBIMycGen98045_0313. DR eggNOG; ENOG4107QN2; Bacteria. DR eggNOG; COG1249; LUCA. DR KO; K00382; -. DR OMA; VYTQPEI; -. DR OrthoDB; EOG6QCD6D; -. DR BioCyc; MGEN243273:GH2R-299-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 InterPro; IPR012999; Pyr_OxRdtase_I_AS. 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. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein; KW Glycolysis; NAD; Oxidoreductase; Redox-active center; KW Reference proteome. FT CHAIN 1 457 Dihydrolipoyl dehydrogenase. FT /FTId=PRO_0000068031. FT NP_BIND 32 40 FAD. {ECO:0000250}. FT NP_BIND 178 182 NAD. {ECO:0000250}. FT NP_BIND 262 265 NAD. {ECO:0000250}. FT ACT_SITE 437 437 Proton acceptor. {ECO:0000250}. FT BINDING 49 49 FAD. {ECO:0000250}. FT BINDING 113 113 FAD; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT BINDING 235 235 NAD; via amide nitrogen. {ECO:0000250}. FT BINDING 303 303 FAD. {ECO:0000250}. FT BINDING 311 311 FAD; via amide nitrogen. {ECO:0000250}. FT DISULFID 40 45 Redox-active. {ECO:0000250}. FT CONFLICT 388 392 FVKMM -> LSRWC (in Ref. 2; AAD10605). FT {ECO:0000305}. SQ SEQUENCE 457 AA; 50119 MW; 2A0B3F11370AD072 CRC64; MDYDLIILGA GPAGYIAAEY AGKHKLKTLV IEKQYFGGVC LNVGCIPTKT LLKRAKIIDY LVHAKDYGIT INGQAKLDWK QLLKQKQEVV DKLVAGVKTI IKGAKVESIE GEATVIDKNK VQVNNTTYTT NNIIVATGSR PRYLTLPGFE KAQQAGFIID STQALALEGV PKKFVVVGGG VIGVEFAFLF ASLGSEVTII QGVDRILEVC DSDVSELISK TLKNKGVQII TNAHVVRAEN NQLFYTVNGV EQSVIGDKIL VSIGRIANTE CLDQLDLKRD HNNKIVLNEK LQTSTTNIYL IGDVNTQMML AHYAYQQGRY AVDQILNQNQ VKPAEKNKCP ACIYTNPEVA FVGYSEMELQ KEKIDYVKSS LPFIYSGKAI ADHETNGFVK MMFNPKTGAI LGGCIIASTA SDIIAELALV MENNLTVFDI ANSISPHPTM NEMVTDVCKK AIFDYFS // ID DNAA_MYCGE Reviewed; 437 AA. AC P35888; Q49363; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 13-APR-2016, entry version 110. DE RecName: Full=Chromosomal replication initiator protein DnaA; GN Name=dnaA; OrderedLocusNames=MG469; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 183-281 AND 286-402. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC72490.1; -; Genomic_DNA. DR EMBL; U02259; AAD12524.1; -; Genomic_DNA. DR EMBL; U02145; AAD12425.1; -; Genomic_DNA. DR PIR; H64251; H64251. DR RefSeq; WP_010869493.1; NC_000908.2. DR PDB; 2JMP; NMR; -; A=1-100. DR PDBsum; 2JMP; -. DR ProteinModelPortal; P35888; -. DR SMR; P35888; 1-100. DR EnsemblBacteria; AAC72490; AAC72490; MG_469. DR KEGG; mge:MG_469; -. DR PATRIC; 20010534; VBIMycGen98045_0540. DR KO; K02313; -. DR OMA; AVGNSIM; -. DR OrthoDB; EOG689HR1; -. DR BioCyc; MGEN243273:GH2R-523-MONOMER; -. DR EvolutionaryTrace; P35888; -. DR Proteomes; UP000000807; 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:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP. DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1750.10; -; 1. DR Gene3D; 3.30.300.20; -; 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; IPR015946; KH_dom-like_a/b. 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 1 437 Chromosomal replication initiator protein FT DnaA. FT /FTId=PRO_0000114211. FT NP_BIND 141 148 ATP. {ECO:0000255}. FT CONFLICT 198 198 E -> G (in Ref. 2; AAD12524). FT {ECO:0000305}. FT HELIX 2 14 {ECO:0000244|PDB:2JMP}. FT HELIX 19 24 {ECO:0000244|PDB:2JMP}. FT TURN 25 28 {ECO:0000244|PDB:2JMP}. FT STRAND 32 34 {ECO:0000244|PDB:2JMP}. FT STRAND 36 42 {ECO:0000244|PDB:2JMP}. FT HELIX 46 54 {ECO:0000244|PDB:2JMP}. FT HELIX 59 62 {ECO:0000244|PDB:2JMP}. FT TURN 63 65 {ECO:0000244|PDB:2JMP}. FT STRAND 71 75 {ECO:0000244|PDB:2JMP}. FT HELIX 77 85 {ECO:0000244|PDB:2JMP}. SQ SEQUENCE 437 AA; 50762 MW; D4DF45A0F4768ED6 CRC64; MEQFNAFKSL LKKHYEKTIG FHDKYIKDIN RFVFKNNVLL ILLENEFARN SLNDNSEIIH LAESLYEGIK SVNFVNEQDF FFNLAKLEEN SRDTLYQNSG LSKNYTFQNF VISEGNKRAY EAGVRLAETQ DNEFSPLFIY GETGLGKTHL LQAIGNEKFR NFPNARVKYV VSSDFAQEVV DAFYQRDKGI EKLKKNYENL DLVLIDDTQI FGRKEKTLEI LFNIFNNLVL NKKQIVLVSD KAPDELIDID ARMISRFKSG LLLKIEKHNL SSLCEILTVK LKEKDPNIQI TNEARHDAAQ ISGNDVRALN GIATKLLFFA KTSKQNLINT ENLKEILFEE FEKFHKKSFD PYLLIENVCR RFNVPMDSVL SENRKAELVR VRDVCNYLLR QKYNMQFQQI GKIFKRSHSS VLMAVKRVAK MIENDSSLRD VITSLVI // ID DNAK_MYCGE Reviewed; 595 AA. AC P47547; Q49321; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 105. 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=MG305; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 353-460. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71527.1; -; Genomic_DNA. DR EMBL; U02204; AAD12493.1; -; Genomic_DNA. DR PIR; G64233; G64233. DR RefSeq; WP_009885883.1; NZ_AAGX01000008.1. DR ProteinModelPortal; P47547; -. DR SMR; P47547; 8-516. DR STRING; 243273.MgenG_010200002514; -. DR PRIDE; P47547; -. DR EnsemblBacteria; AAC71527; AAC71527; MG_305. DR KEGG; mge:MG_305; -. DR PATRIC; 20010140; VBIMycGen98045_0356. DR eggNOG; ENOG4105CFG; Bacteria. DR eggNOG; COG0443; LUCA. DR KO; K04043; -. DR OMA; EKMAPPQ; -. DR OrthoDB; EOG6JMMSV; -. DR BioCyc; MGEN243273:GH2R-341-MONOMER; -. DR Proteomes; UP000000807; 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; 1. 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 1 595 Chaperone protein DnaK. FT /FTId=PRO_0000078490. FT MOD_RES 182 182 Phosphothreonine; by autocatalysis. FT {ECO:0000250}. FT CONFLICT 447 460 PKGKPQIEITFSLD -> LKVNPKLRLPLVWM (in Ref. FT 2). {ECO:0000305}. SQ SEQUENCE 595 AA; 65051 MW; 8EB48D058A009FB7 CRC64; MSADNGLIIG IDLGTTNSCV SVMEGGRPVV LENPEGKRTT PSIVSYKNNE IIVGDAAKRQ MVTNPNTIVS IKRLMGTSNK VKVQNADGTT KELSPEQVSA QILSYLKDFA EKKIGKKISR AVITVPAYFN DAERNATKTA GKIAGLNVER IINEPTAAAL AYGIDKASRE MKVLVYDLGG GTFDVSLLDI AEGTFEVLAT AGDNRLGGDD WDNKIIEYIS AYIAKEHQGL NLSKDKMAMQ RLKEAAERAK IELSAQLETI ISLPFLTVTQ KGPVNVELKL TRAKFEELTK PLLERTRNPI SDVIKEAKIK PEEINEILLV GGSTRMPAVQ KLVESMVPGK KPNRSINPDE VVAIGAAIQG GVLRGDVKDV LLLDVTPLTL SIETLGGVAT PLIKRNTTIP VSKSQIFSTA QDNQESVDVV VCQGERPMSR DNKSLGRFNL GGIQPAPKGK PQIEITFSLD ANGILNVKAK DLTTQKENSI TISDNGNLSE EEIQKMIRDA EANKERDNII RERIELRNEG EGIVNTIKEI LASPDAKNFP KEEKEKLEKL TGNIDAAIKA NDYAKLKVEI ENFKKWREEM AKKYNPTGEQ GPQAK // ID DER_MYCGE Reviewed; 448 AA. AC P47571; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=GTPase Der {ECO:0000255|HAMAP-Rule:MF_00195}; DE AltName: Full=GTP-binding protein EngA {ECO:0000255|HAMAP-Rule:MF_00195}; GN Name=der {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA; GN OrderedLocusNames=MG329; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: GTPase that plays an essential role in the late steps of CC ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}. CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00195}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. EngA (Der) GTPase family. CC {ECO:0000255|HAMAP-Rule:MF_00195}. CC -!- SIMILARITY: Contains 2 EngA-type G (guanine nucleotide-binding) CC domains. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 KH-like domain. {ECO:0000255|HAMAP- CC Rule:MF_00195}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71553.1; -; Genomic_DNA. DR PIR; D64236; D64236. DR RefSeq; WP_009885980.1; NZ_AAGX01000016.1. DR ProteinModelPortal; P47571; -. DR STRING; 243273.MgenG_010200003200; -. DR EnsemblBacteria; AAC71553; AAC71553; MG_329. DR KEGG; mge:MG_329; -. DR PATRIC; 20010214; VBIMycGen98045_0384. DR eggNOG; ENOG4105DKZ; Bacteria. DR eggNOG; COG1160; LUCA. DR KO; K03977; -. DR OMA; DVMGTPI; -. DR OrthoDB; EOG6DC6K1; -. DR BioCyc; MGEN243273:GH2R-377-MONOMER; -. DR Proteomes; UP000000807; 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 SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03594; GTPase_EngA; 1. DR TIGRFAMs; TIGR00231; small_GTP; 2. DR PROSITE; PS51712; G_ENGA; 2. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome; Repeat; Ribosome biogenesis. FT CHAIN 1 448 GTPase Der. FT /FTId=PRO_0000179012. FT DOMAIN 2 169 EngA-type G 1. FT DOMAIN 179 354 EngA-type G 2. FT DOMAIN 355 439 KH-like. {ECO:0000255|HAMAP- FT Rule:MF_00195}. FT NP_BIND 8 15 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 55 59 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 118 121 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 185 192 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 232 236 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 297 300 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. SQ SEQUENCE 448 AA; 50237 MW; C0889F20F7E65CB7 CRC64; MFTVAIIGRT NVGKSTLFNR LIQKPMAIVS DTPNTTRDRI FGIGEWLKRK IAFIDTGGLI AKQTPLQQLI ALQVQAALSQ AKAIIFLVSL QEQLNSDDFY VAKVLKKNKD KPVILVVNKA ENFNPKTAEE TLKDYYSLGF GRPVVISAAH GIGIGDLMDL LVKQNQLLPN ENNDDLAKIR FCVIGKPNVG KSSLINQLVK QNRVLVSNES GTTRDAIDVP LKVNGEKFLL IDTAGIKRKG KINMGIETAS YIKTKLAIAR SNVILLMVDG SKPISEQDEV IGGLAQAALI PVIILVNKWD LVLKNNNTTN AYKKMLKLHF KHLDFAPVLF ISVLKNQRLN TIFEQLKIIQ SQLETKVATP LLNDVIQQAQ LYNQPPLFKG KRLQITYAVQ TKSQIPHFVL FCNDPKYLHF SYARFLENKI RENFGFNSVP ISLYFKSKNA RIRTKPEV // ID DNAJ_MYCGE Reviewed; 389 AA. AC P47265; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=MG019; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71235.1; -; Genomic_DNA. DR EMBL; U01723; AAC43198.1; -; Genomic_DNA. DR PIR; A64202; A64202. DR RefSeq; WP_009885921.1; NZ_AAGX01000010.1. DR ProteinModelPortal; P47265; -. DR STRING; 243273.MgenG_010200002786; -. DR EnsemblBacteria; AAC71235; AAC71235; MG_019. DR KEGG; mge:MG_019; -. DR PATRIC; 20009414; VBIMycGen98045_0017. DR eggNOG; ENOG4105BZ5; Bacteria. DR eggNOG; COG0484; LUCA. DR KO; K03686; -. DR OMA; RVQCATH; -. DR OrthoDB; EOG6BPDKP; -. DR BioCyc; MGEN243273:GH2R-19-MONOMER; -. DR Proteomes; UP000000807; 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 1 389 Chaperone protein DnaJ. FT /FTId=PRO_0000070824. FT DOMAIN 5 79 J. {ECO:0000255|HAMAP-Rule:MF_01152}. FT REPEAT 164 171 CXXCXGXG motif. FT REPEAT 182 189 CXXCXGXG motif. FT REPEAT 208 215 CXXCXGXG motif. FT REPEAT 222 229 CXXCXGXG motif. FT ZN_FING 151 234 CR-type. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT COMPBIAS 84 134 Gly-rich. FT METAL 164 164 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 167 167 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 182 182 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 185 185 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 208 208 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 211 211 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 222 222 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 225 225 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. SQ SEQUENCE 389 AA; 43746 MW; 10614543F4B6ACDE CRC64; MAAGKRDYYE VLGISKNASS QDIKRAFRKL AMQYHPDRHK AENETTQKQN EEKFKEVNEA YEVLSDEEKR KLYDQFGHEG LNASGFHEAG FNPFDIFNSV FGEGFSFGMD GDSPFDFIFN RSKKRQQQIV VPYNLDIALV IEINFFEMTN GCNKTIKYER KVSCHSCNGF GAEGGESGLD LCKDCNGNGF VIKNQRSIFG TIQSQVLCST CNGQGKQIKV KCKTCRSNKY TVTNQIKEIN IPAGMYSGEA LVDESGGNEF KGHYGKLIIQ VNVLASKIFK RSDNNVIANV LVDPMVAIVG GVIELPTLEG IKEFNIRPGT KSGEQIVIPN GGIKFSKSFK RKAGDLIIII SYARPCEYTN LELKKLREFI KPNQEVKQYL NTLKNEYKT // ID DNAB_MYCGE Reviewed; 468 AA. AC P47340; Q49285; Q49456; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 96. DE RecName: Full=Replicative DNA helicase; DE EC=3.6.4.12; GN Name=dnaB; OrderedLocusNames=MG094; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98 AND 267-378. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Participates in initiation and elongation during CC chromosome replication; it exhibits DNA-dependent ATPase activity. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SF4 helicase domain. {ECO:0000255|PROSITE- CC ProRule:PRU00596}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC71312.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAD12440.1; 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; L43967; AAC71312.1; ALT_INIT; Genomic_DNA. DR EMBL; U02158; AAD12440.1; ALT_INIT; Genomic_DNA. DR EMBL; U01803; AAD12329.1; -; Genomic_DNA. DR RefSeq; WP_010869329.1; NC_000908.2. DR ProteinModelPortal; P47340; -. DR STRING; 243273.MgenG_010200000700; -. DR EnsemblBacteria; AAC71312; AAC71312; MG_094. DR KEGG; mge:MG_094; -. DR PATRIC; 20009590; VBIMycGen98045_0104. DR eggNOG; ENOG4105CDU; Bacteria. DR eggNOG; COG0305; LUCA. DR KO; K02314; -. DR OMA; KKASIFR; -. DR OrthoDB; EOG6T4RW5; -. DR BioCyc; MGEN243273:GH2R-97-MONOMER; -. DR Proteomes; UP000000807; Chromosome. 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; IEA:InterPro. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR007694; DNA_helicase_DnaB-like_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF03796; DnaB_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51199; SF4_HELICASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA replication; DNA-binding; KW Helicase; Hydrolase; Nucleotide-binding; Primosome; KW Reference proteome. FT CHAIN 1 468 Replicative DNA helicase. FT /FTId=PRO_0000102025. FT DOMAIN 189 462 SF4 helicase. {ECO:0000255|PROSITE- FT ProRule:PRU00596}. FT NP_BIND 220 227 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00596}. FT CONFLICT 267 270 HESQ -> CMKS (in Ref. 2; AAD12329). FT {ECO:0000305}. SQ SEQUENCE 468 AA; 53884 MW; 88534526DD33561E CRC64; MGQQTSFKYA NDSNIERAER RLMQAVAQNS EGIDLIFNKL EPIDFFATPF KLIFQTAKEN YQLNNPIIGS GLLEAVKFKL DANDQSTKSE LEILFTKILL IRLPPNQTEI KTLVDVVKKA SIFRRLQQFA KRVYNEEFKL KEDRFEGYLQ AIQDDFVKII HSAFSNIFAF SYDEIANQEE ALIKKVHRGE LIISGLSSGF LKLDQLTSGW KPGELIVIAA RPGRGKTALL INFMASAAKQ IDPKTDVVLF FSLEMRNREI YQRHLMHESQ TSYTLTNRQR INNVFEELME ASSRIKNLPI KLFDYSSLTL QEIRNQITEV SKTSNVRLVI IDYLQLVNAL KNNYGLTRQQ EVTMISQSLK AFAKEFNTPI IAAAQLSRRI EERKDSRPIL SDLRESGSIE QDADMVLFIH RTNDDKKEQE EENTNLFEVE LILEKNRNGP NGKVKLNFRS DTSSFISQYS PSFDDQYS // ID DPO3A_MYCGE Reviewed; 874 AA. AC Q49405; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 104. DE RecName: Full=DNA polymerase III subunit alpha; DE EC=2.7.7.7; GN Name=dnaE; OrderedLocusNames=MG261; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71482.1; -; Genomic_DNA. DR PIR; H64228; H64228. DR RefSeq; WP_009885893.1; NZ_AAGX01000009.1. DR ProteinModelPortal; Q49405; -. DR STRING; 243273.MgenG_010200002569; -. DR EnsemblBacteria; AAC71482; AAC71482; MG_261. DR KEGG; mge:MG_261; -. DR PATRIC; 20010020; VBIMycGen98045_0302. DR eggNOG; ENOG4105C0B; Bacteria. DR eggNOG; COG0587; LUCA. DR KO; K02337; -. DR OMA; KNEVELH; -. DR OrthoDB; EOG6CZQGR; -. DR BioCyc; MGEN243273:GH2R-287-MONOMER; -. DR Proteomes; UP000000807; 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; IPR004013; PHP_dom. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR InterPro; IPR004805; PolC_alpha. DR Pfam; PF07733; DNA_pol3_alpha; 1. DR Pfam; PF02811; PHP; 1. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; SSF89550; 1. DR TIGRFAMs; TIGR00594; polc; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA replication; KW DNA-directed DNA polymerase; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 874 DNA polymerase III subunit alpha. FT /FTId=PRO_0000103326. SQ SEQUENCE 874 AA; 100435 MW; 9B27C96A28A74909 CRC64; MFVNLHTNSY YNFLNSALSP KKLVNLAIND QQKAVAITDP NLFGAVEFFI TCKQNNIKPI IGLNLTVEYQ KNDVKLLLIA KSNKGFQTLN KIALIQQKLE INSLVDQLTD IAVIICSLTT WKSTYKDVYQ AKGIEINQTP IAILANAVNC EKTNSDQVVL TVLKQMKQNQ TGKITTFDWD LKQKLNQISI NENLKVKSEI QPFLDQKTAQ QLFSETELNN LNDLVNRCEL DLEHLKAASL SLTDNDAAVL ESLCQTNLKQ FLDKNQDLNK KAYQLRLEKE LNVINKLNFA SYFLVVNDLV NYAFKKDILI GSGRGSAVGS LVAFLLNITK IDPVQHQLIF ERFISTHRQD LPDIDIDIME NKRAEMINYL FEKYGKENCA QIVTFQRFKT RSAVKEVAKL FNDYGISDMI LGVLPKDQTI TFTDLKATED SALQLCLQQF GLIVELALAI VDFPRQSSIH ASGIVIASNS LIKTIPLLQL DNNHFLTQVS MEWLSFFNLN KFDLLGLINL TMISDVITQI KPSNQTVNQF LNTISWTDQN TFINLVNEDT LGIFQLESFG MKKLLVQIKP KTINQLAIVL ALYRPGAQDN INLFINRLHN GYDQSDIDPR ILPIVKNTYG VLIFQEQIIN IVKVVANYSL EEADSFRRAI SKKDVKLIQK NKRNFFERAV QNNFDLKTTT KIFSYIERFA NYGFNLSHAL GYALLSYWTA WLKTNYPVYF YLWLLNHFQS SKDKQKLIIR TLEKSGIEIY PPLLNKAQPN SVIENKKIYL GLNLIKGIND RYIQNLQKVQ HLIQTQNNLQ LTDVVSWCLD KTIGDIPLKD LLLLKTMGCF DFFEYTYDFN DAKDFWIKSD HLLFTRMPLE KKDSNFWIKQ FFTN // ID DNLJ_MYCGE Reviewed; 659 AA. AC P47496; Q49212; Q49213; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 118. 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}; Synonyms=lig; GN OrderedLocusNames=MG254; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-122 AND 477-574. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71474.1; -; Genomic_DNA. DR EMBL; U02152; AAD12433.1; -; Genomic_DNA. DR EMBL; U01761; AAD10575.1; -; Genomic_DNA. DR EMBL; U01761; AAD10576.1; ALT_SEQ; Genomic_DNA. DR PIR; A64228; A64228. DR ProteinModelPortal; P47496; -. DR STRING; 243273.MgenG_010200001742; -. DR EnsemblBacteria; AAC71474; AAC71474; MG_254. DR KEGG; mge:MG_254; -. DR PATRIC; 20009990; VBIMycGen98045_0291. DR eggNOG; ENOG4105C77; Bacteria. DR eggNOG; COG0272; LUCA. DR KO; K01972; -. DR OMA; YITKENF; -. DR OrthoDB; EOG6TTVM9; -. DR BioCyc; MGEN243273:GH2R-276-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. 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; 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; 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; 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; 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 1 659 DNA ligase. FT /FTId=PRO_0000161749. FT DOMAIN 585 655 BRCT. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 32 36 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 81 82 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT ACT_SITE 113 113 N6-AMP-lysine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 398 398 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 401 401 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 416 416 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 421 421 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 111 111 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 134 134 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 168 168 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 280 280 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 304 304 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT CONFLICT 62 72 VGGEAVKGFKK -> WEEKLWRVLKS (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 659 AA; 75388 MW; 1C01E1F49B2A98DC CRC64; MMDVKLKIQQ LVNLIKNYDY HYYVLSEPLI DDFEYDMLYK SLQQLEKDHP DLIQIDSPTQ RVGGEAVKGF KKLNHNSPML SLENAFSTKE IANFIDNINF QTNSKNEFVV EPKIDGVSIS LTYKNGVLVH ALTRGDGSVG EDVLNNVKTI KSIPLTIPFT KTIEIRGEIF VDKKTFLAIN NQLEKPFANA RNLAAGTIRN LNSEITAQRK LRALFYYIPN GLEESITTQT MVLEQLKQWK FPVSDTIRVF QNKFQLINYL EAFDKKREQL TFNLDGLVIK LNSLLFYQQL GATSKSPRWA IAFKFSPKFV QTKLTAVLIT IGRTGRVNYT AKLESVNLDG TKVTAATLHN FDYIKTKDIR INDTVVIYKA GEIIPKVLKV NLEKRKNDTI IIQEQKYCPS CNSKLVKIVD EVDQYCTNET CKERNIQLIN YFVSKTAMDI NGLNINTITK LYEHNLVRSI VDLYDLKDKK NQVLKLDLKI GDKLFNKLVD NIENSKQKGM ARLLTGLGIK HVGNVLAKNL ANHFKNIKAL QHASLENLIS LNDVGITVAE SLYNWFHDPN HLQLIEQLEL RQVKTDQLPL KINFETNSIY FQKRFLITGS FNISRDQIKD LLSAKFDCQF ASEVKPTVDF VIAGNKPTLR KINHAKELNI PIINEAIWT // ID DNAG_MYCGE Reviewed; 607 AA. AC P47492; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 103. 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}; Synonyms=dnaE; GN OrderedLocusNames=MG250; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-216 AND 511-607. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71470.1; -; Genomic_DNA. DR EMBL; U02146; AAD12426.1; -; Genomic_DNA. DR EMBL; U01771; AAD10589.1; -; Genomic_DNA. DR PIR; F64227; F64227. DR RefSeq; WP_009885788.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47492; -. DR STRING; 243273.MgenG_010200001707; -. DR EnsemblBacteria; AAC71470; AAC71470; MG_250. DR KEGG; mge:MG_250; -. DR PATRIC; 20009982; VBIMycGen98045_0287. DR eggNOG; ENOG4105C9G; Bacteria. DR eggNOG; COG0358; LUCA. DR KO; K02316; -. DR OMA; DTHELND; -. DR OrthoDB; EOG6XDGTR; -. DR BioCyc; MGEN243273:GH2R-272-MONOMER; -. DR Proteomes; UP000000807; 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 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 1 607 DNA primase. FT /FTId=PRO_0000180501. FT DOMAIN 267 350 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT ZN_FING 39 63 CHC2-type. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT METAL 273 273 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00974}. FT METAL 319 319 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00974}. FT METAL 319 319 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT METAL 321 321 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00974}. SQ SEQUENCE 607 AA; 71062 MW; A84730CBFA86BDEA CRC64; MVNKSNSLDE LLKQIKITEI IQHYGVKIQT KGNSLLALCP FHDDKNPSMS ISSSKNIFKC WACNAAGNGI AFIQKHDQLD WKTALKKAIE ICGIKLENWN SNLLTKVDPK QKRYWEINNA LITYYQTRLK RETNPNGMNY LVEKRKLNKT LIEQFQLGLA FHNEDKYLCE SMERYPFINP KIKPSELYLF SKTNQQGLGF FDFNTKKATF QNQIMIPIHD FNGNPVGFSA RSVDNINKLK YKNSADHEFF KKGELLFNFH RLNKNLNQLF IVEGYFDVFT LTNSKFEAVA LMGLALNDVQ IKAIKAHFKE LQTLVLALDN DASGQNAVFS LIEKLNNNNF IVEIVQWEHN YKDWDELYLN KGSEQVILQA NKRQNLIEYL VSFFKKQQLD QRVITNKIIA FLTKNQTILN DHSFLIFLIK NLVKLLEYSD EKTLYETVLK HKEKLVSKFD NNRFYINTSG HAQPPQELQK TTAALVQTAF EEAVNELWKP EIFAFALIDK RFLVELKQSH LDEVFKECNF NLFDVELFIE KARIYWSENQ TANWVGFESV LDQNYLLNNK ARLLEIKDIF LDELTCYQAN DFQNYLKTFQ TLLKQQKQRL KNLKLTL // ID DNAJL_MYCGE Reviewed; 310 AA. AC P47248; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=DnaJ-like protein MG002; GN OrderedLocusNames=MG002; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8083173; RA Bailey C.C., Bott K.F.; RT "An unusual gene containing a dnaJ N-terminal box flanks the putative RT origin of replication of Mycoplasma genitalium."; RL J. Bacteriol. 176:5814-5819(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Contains 1 J domain. {ECO:0000255|PROSITE- CC ProRule:PRU00286}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U09251; AAA57070.1; -; Genomic_DNA. DR EMBL; L43967; AAC71218.1; -; Genomic_DNA. DR PIR; B64200; B64200. DR RefSeq; WP_009885561.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47248; -. DR STRING; 243273.MgenG_010200000035; -. DR EnsemblBacteria; AAC71218; AAC71218; MG_002. DR KEGG; mge:MG_002; -. DR PATRIC; 20009380; VBIMycGen98045_0002. DR eggNOG; ENOG4105FTZ; Bacteria. DR eggNOG; COG2214; LUCA. DR OrthoDB; EOG6BPDKP; -. DR BioCyc; MGEN243273:GH2R-2-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 1.10.287.110; -; 1. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR018253; DnaJ_domain_CS. DR Pfam; PF00226; DnaJ; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Reference proteome. FT CHAIN 1 310 DnaJ-like protein MG002. FT /FTId=PRO_0000071000. FT DOMAIN 1 66 J. {ECO:0000255|PROSITE- FT ProRule:PRU00286}. FT CONFLICT 95 95 T -> N (in Ref. 1; AAA57070/AAC71218). FT {ECO:0000305}. SQ SEQUENCE 310 AA; 37365 MW; B61A5C7087FC8BF8 CRC64; MNLYDLLELP TTASIKEIKI AYKRLAKRYH PDVNKLGSQT FVEINNAYSI LSDPNQKEKY DSMLKVNDFQ NRIKNLDISV RWHENFMEEL ELRKTWEFDF FSSDEDFFYS PFTKNKYASF LDKDVSLAFF QLYSKGKIDH QLEKSLLKRR DVKEACQQNK NFIEVIKEQY NYFGWIEAKR YFNINVELEL TQREIRDRDV VNLPLKIKVI NNDFPNQLWY EIYKNYSFRL SWDIKNGEIA EFFNKGNRAL GWKGDLIVRM KVVNKVNKRL RIFSSFFEND KSKLWFLVPN DKQSNPNKGV FNYKTQHFID // ID DNAJM_MYCGE Reviewed; 601 AA. AC P47442; Q49288; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=DnaJ-like protein MG200; GN OrderedLocusNames=MG200; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-409. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Contains 1 J domain. {ECO:0000255|PROSITE- CC ProRule:PRU00286}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71418.1; -; Genomic_DNA. DR EMBL; U02163; AAD12445.1; -; Genomic_DNA. DR PIR; A64222; A64222. DR RefSeq; WP_010869369.1; NC_000908.2. DR PDB; 4DCZ; X-ray; 2.90 A; A/B=124-207. DR PDBsum; 4DCZ; -. DR ProteinModelPortal; P47442; -. DR EnsemblBacteria; AAC71418; AAC71418; MG_200. DR KEGG; mge:MG_200; -. DR PATRIC; 20009852; VBIMycGen98045_0232. DR OrthoDB; EOG6G20RQ; -. DR BioCyc; MGEN243273:GH2R-208-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 1.10.287.110; -; 1. DR InterPro; IPR022466; AGR_box. DR InterPro; IPR002939; DnaJ_C. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR018253; DnaJ_domain_CS. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF01556; DnaJ_C; 1. DR Pfam; PF16713; EAGR_box; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR TIGRFAMs; TIGR03834; EAGR_box; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Chaperone; Complete proteome; Reference proteome. FT CHAIN 1 601 DnaJ-like protein MG200. FT /FTId=PRO_0000071002. FT DOMAIN 5 77 J. {ECO:0000255|PROSITE- FT ProRule:PRU00286}. FT TURN 153 155 {ECO:0000244|PDB:4DCZ}. FT STRAND 163 165 {ECO:0000244|PDB:4DCZ}. FT HELIX 166 170 {ECO:0000244|PDB:4DCZ}. FT TURN 171 174 {ECO:0000244|PDB:4DCZ}. FT TURN 176 178 {ECO:0000244|PDB:4DCZ}. FT STRAND 179 181 {ECO:0000244|PDB:4DCZ}. FT STRAND 187 193 {ECO:0000244|PDB:4DCZ}. FT STRAND 197 201 {ECO:0000244|PDB:4DCZ}. SQ SEQUENCE 601 AA; 68537 MW; F9FAE352E341D093 CRC64; MAEQKRDYYE VLGITPDADQ SEIKKAFRKL AKKYHPDRNN APDAAKIFAE INEANDVLSN PKKRANYDKY GFDGVDGEPA FNFQADVFQS FFEEIAKSGV FNNQTNPEQK EKKKRYHWFS KKPKQEQPEI NLDHVVEQTI KKVQQNQNQN KDPDELRSKV PGEVTASDWE ALVGDTRYGY FDETGDWSWK GYFDEQGKWV WNEPVDSETS EVSVEPEPTP VAPEASFEEA QPEINAEPEA SFESTPTPEP VAPEASFEEA QPEPTPIPEP IPTPVQVQPL LLDLNLFTIP TKATKDDLLF DNINLTTYEQ VVDYLNSQAT PNLAKTDGEL QTIDGTNPLL LEQCKKIKKQ AEQLFKKLFL KKQLPFITQP EVVEESKTSF DENNVNLVYF EKVPEILFIN QQPKEVKYTR QVFDGLTNKT TSETITLEIQ LLQTPKETVS AIFKGFGNDH GKGCGDLKIV FEKIKSPFFQ VNEDGLHSAC IIDPLVAYNG GIIDVFGPYT NFQVKVDGEI DINAIMKFEK LGIAKTKRKG DLFVHLYYSS VPKKKLTTNP QVQQFLELLQ AEYELLQDNI KSLKYFKNNL VIPKKPLDQQ SYQYLSQEPI S // ID DPO3X_MYCGE Reviewed; 597 AA. AC P47658; P47659; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 3. DT 13-APR-2016, entry version 96. DE RecName: Full=DNA polymerase III subunit gamma/tau; DE EC=2.7.7.7; GN Name=dnaX; Synonyms=dnaH, dnaZ; OrderedLocusNames=MG419; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 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 -!- 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 -!- SIMILARITY: Belongs to the DnaX/STICHEL family. {ECO:0000305}. CC -!- CAUTION: Was originally thought to be two separate ORFs named dnaX CC and dnaZ. {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; L43967; AAC71650.2; -; Genomic_DNA. DR PIR; D64246; D64246. DR PIR; T09748; T09748. DR RefSeq; WP_009885609.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47658; -. DR STRING; 243273.MgenG_010200000390; -. DR EnsemblBacteria; AAC71650; AAC71650; MG_419. DR KEGG; mge:MG_419; -. DR PATRIC; 20010426; VBIMycGen98045_0486. DR eggNOG; ENOG4107XK4; Bacteria. DR eggNOG; COG2812; LUCA. DR KO; K02343; -. DR OrthoDB; EOG6WQD76; -. DR BioCyc; MGEN243273:GH2R-474-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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 Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR012763; DNA_pol_III_sug/sutau. DR InterPro; IPR027417; P-loop_NTPase. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF48019; SSF48019; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02397; dnaX_nterm; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA replication; KW DNA-directed DNA polymerase; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 597 DNA polymerase III subunit gamma/tau. FT /FTId=PRO_0000105498. FT NP_BIND 44 51 ATP. {ECO:0000255}. SQ SEQUENCE 597 AA; 69043 MW; DCD8DAF5DBB0323A CRC64; MHQVFYQKYR PINFKQTLGQ ESIRKILVNA INRDKLPNGY IFSGERGTGK TTFAKIIAKA INCLNWDQID VCNSCDVCKS INTNSAIDIV EIDAASKNGI NDIRELVENV FNHPFTFKKK VYILDEAHML TTQSWGGLLK TLEESPPYVL FIFTTTEFNK IPLTILSRCQ SFFFKKITSD LILERLNDIA KKEKIKIEKD ALIKIADLSQ GSLRDGLSLL DQISNFSDSE KISITDVEKT FNIVDRNAKF TFIKAVLSGD IKEAFNLLDD FESNGLNFTY FLRELFALTV NLYAYAKLKN INVLDSTEKT MIETLNFEKQ HYAFLIKAIE ENTNFGLSQL TLIDRLKAIV ISYNEFFNQK PLTISSPSNE KSLHLETEYL EKKKIKKSNH KQDQKHFSLF EKSFIDKSEK TPKNDEVTNN KFLDTSKLNL ANIALAINAF NDNKWINHFQ NLLSVFQTKF NDKDKQNNLS YFNNFIDKYS ARDIVKATKI VKASSFGIVI LFEDQKIAMR LWKEAIEEGN VQATIFQIFN QNLFLASFSE HQYKTTITEE TKNQKYQTEV LNLTQLENLA KPFLKEKKRS LSQKMVDKYF KGLFEEK // ID DPO3_MYCGE Reviewed; 1451 AA. AC P47277; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 109. 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}; OrderedLocusNames=MG031; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 492-567; 975-1103 AND 1111-1225. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA CC polymerase also exhibits 3' to 5' exonuclease activity. CC {ECO:0000255|HAMAP-Rule:MF_00356}. 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; L43967; AAC71247.1; -; Genomic_DNA. DR EMBL; U01807; AAD12336.1; -; Genomic_DNA. DR EMBL; U01712; AAC43185.1; -; Unassigned_DNA. DR EMBL; U02208; AAD12500.1; -; Genomic_DNA. DR PIR; D64203; D64203. DR RefSeq; WP_010869296.1; NC_000908.2. DR ProteinModelPortal; P47277; -. DR EnsemblBacteria; AAC71247; AAC71247; MG_031. DR KEGG; mge:MG_031; -. DR PATRIC; 20009438; VBIMycGen98045_0029. DR KO; K03763; -. DR OMA; QGCTGVK; -. DR OrthoDB; EOG6ZWJJS; -. DR BioCyc; MGEN243273:GH2R-31-MONOMER; -. DR Proteomes; UP000000807; 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:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00356; DNApol_PolC; 1. DR InterPro; IPR011708; DNA_pol3_alpha. DR InterPro; IPR029460; DNAPol_HHH. DR InterPro; IPR006054; DnaQ. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA replication; KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 1451 DNA polymerase III PolC-type. FT /FTId=PRO_0000204582. FT DOMAIN 416 575 Exonuclease. SQ SEQUENCE 1451 AA; 167500 MW; 2DB9E6951F41AAEF CRC64; MVFNLENEKD KKVLALSNFL IDNNILDHNE LNSLIERIES IYFNKYIEEK VFLFAITISR PLTIDIWNAL YEGFNELNEG FKADNESFKL TITFKENEPF FKSKNSFSSV TIAIIKDYFH SFFSKDKKYK ILIEQELSNP NFLSYENDEL KAQCQTKELT EWLVQKSKSF IFWMNNAGFK NFNFIALYPI DKNESKLKVK AVTVSQYDKQ FETKVFATEF IPIHKINQQI DDVKIIGQIF ELKTHESLTG KKTLNIYVTD FQLGGSLILK WSYTDEKKIE GITIGNWIKA HIQVERDPNT QILYGIVREI NPVEIPNNYK RLDLSKQKRV ELVFHTKMTA FDGINDIEEY AQFAKERGWK AITVTDKDNI HIYPKFYEVA KKYDLKAIYG LEFNLTDDHI KIVHNPDNTK LSDATFVIFD IETTGLHGRY DDVIEFSARK IKNNSEIDHQ QFFLKIDKPI PKTITEITKI TDEMLEGGID QQQGLEKIRN YLDDCVMVAH NGINFDLPFL QTQFEKYNIK PLTNPLIDTL CLSWALNPLF SSHTLSNICS KLKLEFDDER LHRAEYDTEA LKKVFFYFKK QLKEMGINTL TEIDQNLNKK CQIDLMKRVF TNTAIVYVKN QRGFQNLYEM LSIALTDHNA NRPLVLASSL AKFRKSFLLT ENPVQGDIFK AALTKPINEL EKAIEKVDFV LISQPNAYLG YTLREGLKKE LINDAIKLVI KTATKLKKLV AVASDAYFIH PWENEYYKAI VCAKGLGGKW HRHFNNKEKE QTVPEVFLHT TDEMLKRMSF LGEDIAYKLV VENTNKIVKL LDLNELVPTK NKLYPPVMQD SNQKLIDKTW KQAEKRYGKN LPKLIKERIE KELNAIISNG FGIVFWISHL LVEQSVKDGY FVGPRGSIGS SLIANLIGIS EINPLAAHYL CEQCHYFEVS DSVDDGYDLM IRDCPKCHEK ASFKGDGHNI PFATFMGFSG DKIPDIDLNF SSEYQAKAHD YVRKLFGVNN TFRAGTIATV AEKTAYGYAR NYFEIIKRVD LATTAEIERF KQKLIGIKRT TGQHPGGIMI FPSDHSVYEF TPCGFPADDV ESEWKTTHFE YDALGDAILK LDILGQDDPT MLKHLADLTK INPQNIPHFD KNLISMFSSN KPLNLKPGIV DEVTGAVGIP EFGTKFVRKI LEQTKPKDFA DLIRVSGLSH GKNVWADNAQ KLIKSNRLTL RDVIACRDDI MLYLINKGMQ AKDAFEIMEK VRKGIKVNAK EVSLMQNCGV EQYWINACLK INYLFPKAHA AAYVLMAWRI AWFKLYHPLS YYACLLSFKL KEHDINGFEK GYEFIKNRLD ELNKLYRIKK IKPKEAELLT SYEVYLEMMA RNIKLQQISI QNSNARMFVE HNGVLIAPFI TIPGMGEAVA SSIVEARNEK PFASLNDFKK RTKITKKHVE TMEQLQLFDE FEHQDDHKLF N // ID ECFA1_MYCGE Reviewed; 274 AA. AC P47425; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 109. 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=cbiO1; GN OrderedLocusNames=MG179; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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. {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter CC complex composed of 2 membrane-embedded substrate-binding proteins CC (S component), 2 ATP-binding proteins (A component) and 2 CC transmembrane proteins (T component). {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01710}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01710}. 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; L43967; AAC71398.1; -; Genomic_DNA. DR PIR; H64219; H64219. DR RefSeq; WP_009885864.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47425; -. DR STRING; 243273.MgenG_010200002299; -. DR EnsemblBacteria; AAC71398; AAC71398; MG_179. DR KEGG; mge:MG_179; -. DR PATRIC; 20009790; VBIMycGen98045_0201. DR eggNOG; ENOG4108JJB; Bacteria. DR eggNOG; COG1122; LUCA. DR KO; K16786; -. DR OMA; SIISITH; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-188-MONOMER; -. DR Proteomes; UP000000807; 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:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; 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; IPR015856; ABC_transpr_CbiO/EcfA_su. DR InterPro; IPR030947; EcfA_1. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR04520; ECF_ATPase_1; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51246; CBIO; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 274 Energy-coupling factor transporter ATP- FT binding protein EcfA1. FT /FTId=PRO_0000092036. FT DOMAIN 9 240 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01710}. FT NP_BIND 41 48 ATP. {ECO:0000255|HAMAP-Rule:MF_01710}. SQ SEQUENCE 274 AA; 30545 MW; 5A70BD912AF054B1 CRC64; MLPTKQAACS FINVAFSYNE LPLIRELSFS VYEGEYVCIV GHNGSGKSTI SKLLTGLLKP QAGEIKIFGK TVDFDNVSYL RNNIGIIFQN PDNQFIGITV EDDIAFGLEN KCFSRQKIKA IIDEVTLQTQ TDGFIKQEPH NLSGGQKQRV AIASVLALNP AIIIFDESTA MLDPKAKKTI KQFMVKLAKQ GKCVISITHD MEEVTKADKV LVMNEGKLIK QGKPVEVFTS EQELQKIRLD IPFSLSLSTK IRGITSTIDY QTLIKSIAKL WKKR // ID EFG_MYCGE Reviewed; 688 AA. AC P47335; Q49196; Q49265; Q49303; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Elongation factor G; DE Short=EF-G; GN Name=fusA; Synonyms=fus; OrderedLocusNames=MG089; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 230-458; 514-626 AND 629-688. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71307.1; -; Genomic_DNA. DR EMBL; U01722; AAC43197.1; -; Unassigned_DNA. DR EMBL; U02180; AAD12466.1; -; Genomic_DNA. DR EMBL; U02136; AAD12412.1; -; Genomic_DNA. DR PIR; H64209; H64209. DR RefSeq; WP_009885646.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47335; -. DR SMR; P47335; 5-684. DR STRING; 243273.MgenG_010200000665; -. DR EnsemblBacteria; AAC71307; AAC71307; MG_089. DR KEGG; mge:MG_089; -. DR PATRIC; 20009580; VBIMycGen98045_0099. DR eggNOG; ENOG4105CEJ; Bacteria. DR eggNOG; COG0480; LUCA. DR KO; K02355; -. DR OMA; KLGVAIQ; -. DR OrthoDB; EOG6X6RBF; -. DR BioCyc; MGEN243273:GH2R-92-MONOMER; -. DR Proteomes; UP000000807; 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:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. 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 1 688 Elongation factor G. FT /FTId=PRO_0000091156. FT DOMAIN 8 282 tr-type G. FT NP_BIND 17 24 GTP. {ECO:0000250}. FT NP_BIND 81 85 GTP. {ECO:0000250}. FT NP_BIND 135 138 GTP. {ECO:0000250}. FT CONFLICT 345 346 NK -> KQ (in Ref. 2; AAC43197). FT {ECO:0000305}. FT CONFLICT 514 514 N -> M (in Ref. 2). {ECO:0000305}. FT CONFLICT 657 657 S -> Y (in Ref. 2; AAD12412). FT {ECO:0000305}. SQ SEQUENCE 688 AA; 76539 MW; 4D906162F123B690 CRC64; MSRTVDLKNF RNFGIMAHID AGKTTTSERI LFHSGRIHKI GETHDGESVM DWMEQEKERG ITITSAATSV SWKNCSLNLI DTPGHVDFTV EVERSLRVLD GAIAVLDAQM GVEPQTETVW RQASRYEVPR VIFVNKMDKT GANFERSVLS IQQRLGVKAV PIQFPIGAEN DFNGIIDIIT KKAYFFDGNK EENAIEKPIP EQYVDQVEKL YNNLVEEVAS LDDQLMADYL DGKPIEIDAI KNAIRNGVIH CKFFPVLCGS AFKNKGIKLL LDAVVDFLPS PVDVPPAKAI DANNKEISIK ASDDANFIGL AFKVATDPFV GRLTFIRVYA GVLKSGSYVK NVRKNKKERV SRLVKMHAQN RNEIDEIRAG DICAVIGLKD TTTGETLTDD KLDVQLEAMQ FAEPVISLAV EPKTKADQEK MSIALSKLAE EDPTFKTFSD PETGQTIIAG MGELHLDILV DRMKREFKVE VNIGAPQVSF RETFKSTSEV EGKYIKQSGG RGQYGHVKIR FEPNKDKGFE FVDKIVGGRI PREYIKPVQT GLENAMNSGP LAGYPMIDIK ATLFDGSFHE VDSSEMAFKI AASLALKEAG KQCNPVLLEP IMAIEVTVPE QYFGDTMGDI SSRRGIIEGT EQRDNVQLIK AKVPLKEMFG YATDLRSFSQ GRGNYVMQFS HYAETPKSVV NEIIANKK // ID DPO3B_MYCGE Reviewed; 364 AA. AC P47247; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 96. DE RecName: Full=DNA polymerase III subunit beta; DE EC=2.7.7.7; GN Name=dnaN; OrderedLocusNames=MG001; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 267-364. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8083173; RA Bailey C.C., Bott K.F.; RT "An unusual gene containing a dnaJ N-terminal box flanks the putative RT origin of replication of Mycoplasma genitalium."; RL J. Bacteriol. 176:5814-5819(1994). 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 (By similarity). {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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71217.1; -; Genomic_DNA. DR EMBL; U09251; AAA57069.1; -; Genomic_DNA. DR ProteinModelPortal; P47247; -. DR STRING; 243273.MgenG_010200000040; -. DR EnsemblBacteria; AAC71217; AAC71217; MG_001. DR KEGG; mge:MG_001; -. DR PATRIC; 20009378; VBIMycGen98045_0001. DR eggNOG; ENOG410885N; Bacteria. DR eggNOG; COG0592; LUCA. DR KO; K02338; -. DR OMA; NADANFE; -. DR OrthoDB; EOG65J53F; -. DR BioCyc; MGEN243273:GH2R-1-MONOMER; -. DR Proteomes; UP000000807; 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; IPR022634; DNA_polIII_beta_N. DR Pfam; PF00712; DNA_pol3_beta; 1. DR Pfam; PF02768; DNA_pol3_beta_3; 1. DR SMART; SM00480; POL3Bc; 1. DR TIGRFAMs; TIGR00663; dnan; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA replication; KW DNA-directed DNA polymerase; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 364 DNA polymerase III subunit beta. FT /FTId=PRO_0000105445. SQ SEQUENCE 364 AA; 42399 MW; 4D8C23EF9BC48624 CRC64; MNNVIISNNK IKPHHSYFLI EAKEKEINFY ANNEYFSVKC NLNKNIDILE QGSLIVKGKI FNDLINGIKE EIITIQEKDQ TLLVKTKKTS INLNTINVNE FPRIRFNEKN DLSEFNQFKI NYSLLVKGIK KIFHSVSNNR EISSKFNGVN FNGSNGKEIF LEASDTYKLS VFEIKQETEP FDFILESNLL SFINSFNPEE DKSIVFYYRK DNKDSFSTEM LISMDNFMIS YTSVNEKFPE VNYFFEFEPE TKIVVQKNEL KDALQRIQTL AQNERTFLCD MQINSSELKI RAIVNNIGNS LEEISCLKFE GYKLNISFNP SSLLDHIESF ESNEINFDFQ GNSKYFLITS KSEPELKQIL VPSR // ID EFTS_MYCGE Reviewed; 298 AA. AC P47246; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 104. DE RecName: Full=Elongation factor Ts; DE Short=EF-Ts; GN Name=tsf; OrderedLocusNames=MG433; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC72454.1; -; Genomic_DNA. DR PIR; H64247; H64247. DR RefSeq; WP_009885600.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47246; -. DR STRING; 243273.MgenG_010200000295; -. DR EnsemblBacteria; AAC72454; AAC72454; MG_433. DR KEGG; mge:MG_433; -. DR PATRIC; 20010452; VBIMycGen98045_0499. DR eggNOG; ENOG4105CU7; Bacteria. DR eggNOG; COG0264; LUCA. DR KO; K02357; -. DR OMA; FIMEPKK; -. DR OrthoDB; EOG66B42N; -. DR BioCyc; MGEN243273:GH2R-487-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.479.20; -; 3. 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; 2. 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 1 298 Elongation factor Ts. FT /FTId=PRO_0000161151. FT REGION 79 82 Involved in Mg(2+) ion dislocation from FT EF-Tu. {ECO:0000250}. SQ SEQUENCE 298 AA; 34265 MW; 014E423EBD2A5F7B CRC64; MATKIELIKE LRKSTQASVM DCKQALEKNN DDFEKAVKWL RENGIVKSTK KLNKVASEGI IVLKSNLHKA IMVEINSQTD FVAKNQELKE FSDLMLEKIF EKVNPKTELV EIEKIQINND EKVSEKLALI ASKTDEKIVL RRVVVFETKT NQIFTYLHAN KRIGVIIEIQ GKLNEDDGKH LAMHIAANSP QFIDQSDVNQ TWLQNERNII RSQAELEVKE NPKKAIFLEK TIEGRVNKLL IDTCLINQKY LIDETKTIGQ FLKEKQAKVL KFIRYEVGEG IIKETVDFVS EVNAQIKQ // ID END4_MYCGE Reviewed; 291 AA. AC P47477; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 103. 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=MG235; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71456.1; -; Genomic_DNA. DR PIR; I64225; I64225. DR RefSeq; WP_009885772.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47477; -. DR STRING; 243273.MgenG_010200001602; -. DR EnsemblBacteria; AAC71456; AAC71456; MG_235. DR KEGG; mge:MG_235; -. DR PATRIC; 20009952; VBIMycGen98045_0272. DR eggNOG; ENOG4105EFU; Bacteria. DR eggNOG; COG0648; LUCA. DR KO; K01151; -. DR OMA; IYLGAPQ; -. DR OrthoDB; EOG6Z0QCM; -. DR BioCyc; MGEN243273:GH2R-257-MONOMER; -. DR Proteomes; UP000000807; 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:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. 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 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; Endonuclease; Hydrolase; KW Metal-binding; Nuclease; Reference proteome; Zinc. FT CHAIN 1 291 Probable endonuclease 4. FT /FTId=PRO_0000190852. FT METAL 72 72 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 112 112 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 147 147 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 147 147 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 181 181 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 184 184 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}. SQ SEQUENCE 291 AA; 32391 MW; C6A4FE04247CF9F4 CRC64; MPKLLGSFIS FKAPNYFVQS AQDAIAIDAT ALMVFLGPPH SAYRVPFNKM QFSLGYELLK TKNINSNGLV VHAPYIINCA SKDPLKQQNA ISVLTNEIQL CNLAGAHYLV LHPGSAVAQT TNEALDNLVK VLNQVINKTK TTVICLETMA GKGNEIGRDL TELKYVIDRI VDKDRIGVCL DTCHFHDSGI DFSDLTGVFN TITTKLGFEF LKVIHLNESK NNCGSKKDRH ANINAGMIGF ENLMKFISHP QIKDLPIILE TPSTSLNYPT IYREEISQIR SWFKTYQPDA N // ID DYR_MYCGE Reviewed; 160 AA. AC P47470; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Dihydrofolate reductase; DE EC=1.5.1.3; GN Name=folA; Synonyms=dhfR; OrderedLocusNames=MG228; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; CC 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71449.1; -; Genomic_DNA. DR PIR; B64225; B64225. DR RefSeq; WP_009885765.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47470; -. DR STRING; 243273.MgenG_010200001567; -. DR EnsemblBacteria; AAC71449; AAC71449; MG_228. DR KEGG; mge:MG_228; -. DR PATRIC; 20009938; VBIMycGen98045_0265. DR eggNOG; ENOG41084DH; Bacteria. DR eggNOG; COG0262; LUCA. DR KO; K00287; -. DR OMA; IISIWAM; -. DR OrthoDB; EOG6KT2V2; -. DR BioCyc; MGEN243273:GH2R-250-MONOMER; -. DR UniPathway; UPA00077; UER00158. DR Proteomes; UP000000807; 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; IPR017925; DHFR_CS. DR InterPro; IPR001796; DHFR_dom. DR Pfam; PF00186; DHFR_1; 1. DR PRINTS; PR00070; DHFR. DR SUPFAM; SSF53597; SSF53597; 1. DR PROSITE; PS00075; DHFR_1; 1. DR PROSITE; PS51330; DHFR_2; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; One-carbon metabolism; Oxidoreductase; KW Reference proteome. FT CHAIN 1 160 Dihydrofolate reductase. FT /FTId=PRO_0000186395. FT DOMAIN 1 160 DHFR. {ECO:0000255|PROSITE- FT ProRule:PRU00660}. FT NP_BIND 6 7 NADP. {ECO:0000250}. FT NP_BIND 14 19 NADP. {ECO:0000250}. FT NP_BIND 43 46 NADP. {ECO:0000250}. FT NP_BIND 62 65 NADP. {ECO:0000250}. FT NP_BIND 101 106 NADP. {ECO:0000250}. FT REGION 5 7 Substrate binding. {ECO:0000250}. FT BINDING 27 27 Substrate. {ECO:0000250}. FT BINDING 57 57 Substrate. {ECO:0000250}. FT BINDING 120 120 Substrate. {ECO:0000250}. SQ SEQUENCE 160 AA; 18966 MW; BE46EBAE24DDBE13 CRC64; MLIAIWAMTQ EGLIGNNNTL PWMIKQELAH FKKTTLFQAL LMGRKTYESL PKVFEKRTIF LLSKDQNYRF EEKGSEVKVI NDFWPLIKSY QANKEKDLFI CGGKSVYEQT INECDQLIVS IIKKKYKGDQ FLKVDLSKFV LNEVVEFEEF NVNYYRKKQQ // ID ECFA2_MYCGE Reviewed; 304 AA. AC P47426; Q49207; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA2 {ECO:0000255|HAMAP-Rule:MF_01710}; DE Short=ECF transporter A component EcfA2 {ECO:0000255|HAMAP-Rule:MF_01710}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01710}; GN Name=ecfA2 {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO2; GN OrderedLocusNames=MG180; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-83 AND 262-304. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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. {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter CC complex composed of 2 membrane-embedded substrate-binding proteins CC (S component), 2 ATP-binding proteins (A component) and 2 CC transmembrane proteins (T component). {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01710}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01710}. 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; L43967; AAC71399.1; -; Genomic_DNA. DR EMBL; U01754; AAD10568.1; -; Genomic_DNA. DR EMBL; U01750; AAD10564.1; -; Genomic_DNA. DR PIR; I64219; I64219. DR RefSeq; WP_009885865.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47426; -. DR STRING; 243273.MgenG_010200002304; -. DR EnsemblBacteria; AAC71399; AAC71399; MG_180. DR KEGG; mge:MG_180; -. DR PATRIC; 20009792; VBIMycGen98045_0202. DR eggNOG; ENOG4108JJB; Bacteria. DR eggNOG; COG1122; LUCA. DR KO; K16787; -. DR OMA; DRVGLKH; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-189-MONOMER; -. DR Proteomes; UP000000807; 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:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; 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; IPR015856; ABC_transpr_CbiO/EcfA_su. DR InterPro; IPR030946; EcfA2. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR04521; ECF_ATPase_2; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51246; CBIO; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 304 Energy-coupling factor transporter ATP- FT binding protein EcfA2. FT /FTId=PRO_0000092037. FT DOMAIN 11 260 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01710}. FT NP_BIND 54 61 ATP. {ECO:0000255|HAMAP-Rule:MF_01710}. FT CONFLICT 11 14 LKAD -> FKSS (in Ref. 2; AAD10568). FT {ECO:0000305}. SQ SEQUENCE 304 AA; 34385 MW; 32B05A81138DCA82 CRC64; MKKKIVPINP LKADEILAVS HLSCVFNSKT NNPIKVIDDF SYTFQKNQIY CIIGDSGSGK STLVNHFNGL IKPNQGDIWV KDIYIGAKQR KIKNFKKLRK TISIVFQFPE YQLFKDTVEK DIMFGPVALG QSKYDARQKA AYYLEMMGLK YPFLERNPFE LSGGQKRRVA IAGILAIEPE ILIFDEPTAG LDPEGEREMM QLIKTAKQQQ RTVFMITHQM ENVLEVADVV LVLAKGKLVK AASPYEVFMD QTFLEKTTIV LPPVIQVIKD LIAINAHFNK LIELQPKNLE QLASAINKTI ANHG // ID EFP_MYCGE Reviewed; 190 AA. AC P47272; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Elongation factor P; DE Short=EF-P; GN Name=efp; OrderedLocusNames=MG026; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-87. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71242.1; -; Genomic_DNA. DR EMBL; U02253; AAD12518.1; -; Genomic_DNA. DR PIR; H64202; H64202. DR RefSeq; WP_010869294.1; NC_000908.2. DR ProteinModelPortal; P47272; -. DR EnsemblBacteria; AAC71242; AAC71242; MG_026. DR KEGG; mge:MG_026; -. DR PATRIC; 20009428; VBIMycGen98045_0024. DR KO; K02356; -. DR OMA; DRRDYQY; -. DR OrthoDB; EOG6JQH6Q; -. DR BioCyc; MGEN243273:GH2R-26-MONOMER; -. DR UniPathway; UPA00345; -. DR Proteomes; UP000000807; 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 1 190 Elongation factor P. FT /FTId=PRO_0000094283. SQ SEQUENCE 190 AA; 21914 MW; C7510FB5DF94FFB9 CRC64; MAEMIEAKNL RNGQTIFGPN KEILLVLENT FNKTAMRQGI VKTKVKNLRT GAIVWLEFTG DKLEQVIIDK KKMNFLYKDG NNFVFMDQKD YSQIEINEKK LEWEKNFITE EIEVTVITYQ DEILGVNLPD LVPIEVEFAE DAIQGNTANM ARKKARLVTG YELDVPQFIN TGDKIVIATV DGNYRERFNK // ID EFTU_MYCGE Reviewed; 394 AA. AC P13927; Q49360; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 13-APR-2016, entry version 114. 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=MG451; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=2602130; DOI=10.1093/nar/17.23.10127; RA Inamine J.M., Loechel S., Hu P.-C.; RT "Nucleotide sequence of the tuf gene from Mycoplasma genitalium."; RL Nucleic Acids Res. 17:10127-10127(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 196-309. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; X16463; CAA34483.1; -; Genomic_DNA. DR EMBL; L43967; AAC72471.1; -; Genomic_DNA. DR EMBL; U02255; AAD12520.1; -; Genomic_DNA. DR PIR; S14909; EFYMTG. DR RefSeq; WP_009885583.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P13927; -. DR SMR; P13927; 2-393. DR STRING; 243273.MgenG_010200000185; -. DR PRIDE; P13927; -. DR EnsemblBacteria; AAC72471; AAC72471; MG_451. DR KEGG; mge:MG_451; -. DR PATRIC; 20010492; VBIMycGen98045_0519. DR eggNOG; ENOG4105CGV; Bacteria. DR eggNOG; COG0050; LUCA. DR KO; K02358; -. DR OMA; GMVICKP; -. DR OrthoDB; EOG6R5C6X; -. DR BioCyc; MGEN243273:GH2R-504-MONOMER; -. DR Proteomes; UP000000807; 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:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. 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 1 394 Elongation factor Tu. FT /FTId=PRO_0000091346. FT DOMAIN 10 204 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 220 220 T -> N (in Ref. 3; AAD12520). FT {ECO:0000305}. SQ SEQUENCE 394 AA; 42990 MW; 3F62C644A40E49DA CRC64; MAREKFDRSK PHVNVGTIGH IDHGKTTLTA AICTVLAKEG KSAATRYDEI DKAPEEKARG ITINSAHVEY SSDKRHYAHV DCPGHADYIK NMITGAAQMD GAILVVSATD SVMPQTREHI LLARQVGVPK MVVFLNKCDI ASDEEVQELV AEEVRDLLTS YGFDGKNTPI IYGSALKALE GDPKWEAKIH DLIKAVDEWI PTPTREVDKP FLLAIEDTMT ITGRGTVVTG RVERGELKVG QEVEIVGLKP IRKAVVTGIE MFKKELDSAM AGDNAGVLLR GVERKEVERG QVLAKPGSIK PHKKFKAEIY ALKKEEGGRH TGFLNGYRPQ FYFRTTDVTG SIALAENTEM VLPGDNASIT VELIAPIACE KGSKFSIREG GRTVGAGTVT EVLE // ID ENGB_MYCGE Reviewed; 191 AA. AC P47577; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321}; GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=MG335; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71558.1; -; Genomic_DNA. DR PIR; A64237; A64237. DR RefSeq; WP_010869438.1; NC_000908.2. DR ProteinModelPortal; P47577; -. DR STRING; 243273.MgenG_010200003101; -. DR EnsemblBacteria; AAC71558; AAC71558; MG_335. DR KEGG; mge:MG_335; -. DR PATRIC; 20010226; VBIMycGen98045_0390. DR eggNOG; ENOG4105WHM; Bacteria. DR eggNOG; COG0218; LUCA. DR KO; K03978; -. DR OMA; DYIMIEY; -. DR OrthoDB; EOG6ND0NG; -. DR BioCyc; MGEN243273:GH2R-383-MONOMER; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; GTP-binding; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Septation. FT CHAIN 1 191 Probable GTP-binding protein EngB. FT /FTId=PRO_0000157763. FT DOMAIN 19 188 EngB-type G. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT NP_BIND 27 34 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 53 57 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 70 73 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 136 139 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 167 169 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT METAL 34 34 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT METAL 55 55 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. SQ SEQUENCE 191 AA; 21835 MW; 7326A58A2F8C5F07 CRC64; MDAHFLKSAS DLKDCPQDNI PEICFMGRSN VGKSSLINAF FKKKLAKTSA TPGRTQLLNY FEYKDKRFVD LPGYGFAKIN KNKKDFITNL LTQFLNFRSN LVGVVLIVDS GVVTVQDQEV VKIILQTGLN FLIVANKFDK LNQSERYFSL KNIANFLKVN FDKCVFASTK THHNLALVHK KIFELFVEDE R // ID ENO_MYCGE Reviewed; 458 AA. AC P47647; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 116. 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=MG407; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(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}. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + CC H(2)O. {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00318}; 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. {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP- CC Rule:MF_00318}. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71635.1; -; Genomic_DNA. DR PIR; A64245; A64245. DR RefSeq; WP_009885616.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47647; -. DR SMR; P47647; 10-453. DR STRING; 243273.MgenG_010200000455; -. DR EnsemblBacteria; AAC71635; AAC71635; MG_407. DR KEGG; mge:MG_407; -. DR PATRIC; 20010406; VBIMycGen98045_0476. DR eggNOG; ENOG4105C70; Bacteria. DR eggNOG; COG0148; LUCA. DR KO; K01689; -. DR OMA; EFMIIPV; -. DR OrthoDB; EOG65J589; -. DR BioCyc; MGEN243273:GH2R-464-MONOMER; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000000807; 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; 2. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; KW Metal-binding; Reference proteome; Secreted. FT CHAIN 1 458 Enolase. FT /FTId=PRO_0000133923. FT REGION 389 392 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 219 219 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 362 362 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 256 256 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 310 310 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 337 337 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 169 169 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 178 178 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 310 310 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 337 337 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 362 362 Substrate (covalent); in inhibited form. FT {ECO:0000255|HAMAP-Rule:MF_00318}. FT BINDING 413 413 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. SQ SEQUENCE 458 AA; 50019 MW; 4007A37ADD9EE9FF CRC64; MGSSNLNINS KITDIFAYQV FDSRGVPTVA CVVKLASGHV GEAMVPSGAS TGEKEAIELR DNDPKNYFGK GVNEAVDNVN KVIAPKLIGL NAFDQLTVDQ AMIKLDNTPN KAKLGANAIL SVSLAVSKAA AKAQNSSLFQ YISNKLIGLN TTNFVLPVPM LNVINGGAHA DNYIDFQEFM IMPLGAKKMH EALKMASETF HALQNLLKKR GLNTNKGDEG GFAPNLKLAE DALDIMVEAI KLAGYKPWDD IAIAIDVAAS EFYDEDKKLY VFKKGIKANI LNAKDWSLTS KEMIAYLEKL TKKYPIISIE DGLSENDWEG MNQLTKTIGS HIQIVGDDTY CTNAELAKKG VAQNTTNSIL IKLNQIGSIS ETIQTIEVAK KANWSQVISH RSGETEDTTI ADLAVAAQTG QIKTGSMSRS ERIAKYNRLL YIEIELGDKG KYLGWNTFTN IKPKNFNI // ID ERA_MYCGE Reviewed; 290 AA. AC P47627; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367}; GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; Synonyms=spg; GN OrderedLocusNames=MG387; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 membrane {ECO:0000255|HAMAP- CC Rule:MF_00367}; Peripheral membrane protein {ECO:0000255|HAMAP- CC 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; L43967; AAC71614.1; -; Genomic_DNA. DR PIR; H64242; H64242. DR RefSeq; WP_010869462.1; NC_000908.2. DR ProteinModelPortal; P47627; -. DR EnsemblBacteria; AAC71614; AAC71614; MG_387. DR KEGG; mge:MG_387; -. DR PATRIC; 20010360; VBIMycGen98045_0453. DR KO; K03595; -. DR OMA; HIRTTIM; -. DR OrthoDB; EOG693GPD; -. DR BioCyc; MGEN243273:GH2R-444-MONOMER; -. DR Proteomes; UP000000807; 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 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 membrane; Complete proteome; Cytoplasm; GTP-binding; Membrane; KW Nucleotide-binding; Reference proteome; Ribosome biogenesis; KW RNA-binding; rRNA-binding. FT CHAIN 1 290 GTPase Era. FT /FTId=PRO_0000180027. FT DOMAIN 2 144 Era-type G. FT DOMAIN 201 279 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_00367}. FT NP_BIND 10 17 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. FT NP_BIND 58 62 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. FT NP_BIND 122 125 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. SQ SEQUENCE 290 AA; 33722 MW; 96EB817D724A0CB9 CRC64; MKVLKVGVLG PTNAGKSTLI NFLHNDDSLM VSSMNNTTLL SISTEVINQA NKNIVFIDVP GFTEKKHSNY ELITKEIRKA LSGIDVLLLV VRSDQNNKIE FLKTQLQQLK RYQNLTRIFL INKFHQKSLS EVNKAIILEE FKPQKTIEIN LLKFDKNLFW SIFKQVELRY NIFRKDINFI DANNDDFKIL EGLREQIIFY CKNEIPHIAR IEIIEKSFNK EKNLLKIHLV ISVPKLSQKK IIIGKNAEMI KAIGIATRKK LLNHFDCDIF IDIFVKTEKQ KLPVYSFLSK // ID ESL1_MYCGE Reviewed; 268 AA. AC Q49412; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=Putative esterase/lipase 1; DE EC=3.1.-.-; GN OrderedLocusNames=MG310; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO 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; L43967; AAC71532.1; -; Genomic_DNA. DR PIR; C64234; C64234. DR RefSeq; WP_009885888.1; NZ_AAGX01000008.1. DR ProteinModelPortal; Q49412; -. DR STRING; 243273.MgenG_010200002539; -. DR ESTHER; mycge-esl1; AlphaBeta_hydrolase. DR EnsemblBacteria; AAC71532; AAC71532; MG_310. DR KEGG; mge:MG_310; -. DR PATRIC; 20010150; VBIMycGen98045_0361. DR eggNOG; COG0596; LUCA. DR OMA; RALIYNI; -. DR OrthoDB; EOG6D2KXC; -. DR BioCyc; MGEN243273:GH2R-346-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW. 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; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome; Serine esterase. FT CHAIN 1 268 Putative esterase/lipase 1. FT /FTId=PRO_0000207074. FT ACT_SITE 27 27 {ECO:0000255}. FT ACT_SITE 94 94 Charge relay system. {ECO:0000250}. SQ SEQUENCE 268 AA; 30747 MW; 7300775DAD753376 CRC64; MRLEIENGLE FVNDPVVNEL GKICFFHPFT GNLTNKLSFR SHFNRYSFYA INYPGHGNSV INNPKQLEFS YWLEITKQFF DKHNLKDVIL FGHSIGGGLA VALTNYLSSD QYKAVLLEAP LNPAIVETPL NIVQNLIPDP DSDFAVIQKC LVYNIEKKLG ANFKEYCERE KQKSIHQNQR LKVMLEPSTL KQNIVLINAA FLKLNCPALW IHGKQDGIIK YLPSKAYYES LNNKQIQFKA IEAAAHTPYF EQPQKFLSLV NDFFQLIS // ID ESL2_MYCGE Reviewed; 268 AA. AC Q49418; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 86. DE RecName: Full=Putative esterase/lipase 2; DE EC=3.1.-.-; GN OrderedLocusNames=MG327; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO 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; L43967; AAC71551.1; -; Genomic_DNA. DR PIR; B64236; B64236. DR RefSeq; WP_010869433.1; NC_000908.2. DR ProteinModelPortal; Q49418; -. DR STRING; 243273.MgenG_010200003073; -. DR ESTHER; mycge-esl2; AlphaBeta_hydrolase. DR EnsemblBacteria; AAC71551; AAC71551; MG_327. DR KEGG; mge:MG_327; -. DR PATRIC; 20010210; VBIMycGen98045_0382. DR eggNOG; COG0596; LUCA. DR OMA; ERAYEMI; -. DR OrthoDB; EOG6D2KXC; -. DR BioCyc; MGEN243273:GH2R-375-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome; Serine esterase. FT CHAIN 1 268 Putative esterase/lipase 2. FT /FTId=PRO_0000207076. FT ACT_SITE 29 29 {ECO:0000255}. FT ACT_SITE 98 98 Charge relay system. {ECO:0000250}. SQ SEQUENCE 268 AA; 30700 MW; C8DFADB6A41D6087 CRC64; MLTSNKNTLF NSIFAFKPKK RKNVFIFLHG FGSEYASFSR IFSLFKKKKW PFFTFNFPGH GDNESTDTDQ LKLNHFVDLV CDFIVQKKLN NVILIGHSMG GAVAVLVNKV IPLKIKALIL VAPMNQTSFS VNKKRILDTF FKRNNSNHKD FVEHEEKRKS LLKIAINAFK KRTTFKTLYS DMVQNAKYGN DSLERAYEMI GNKPTLVILG ANDIVTPTKA SVDYLANKSD KIIFKVIDGV GHSPHDSAPK LFFDYVLEFL DNLKKQRY // ID EX53_MYCGE Reviewed; 291 AA. AC Q49406; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=5'-3' exonuclease; DE EC=3.1.11.-; GN Name=polA; OrderedLocusNames=MG262; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: 5'-3' exonuclease acting preferentially on double- CC stranded DNA. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 5'-3' 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; L43967; AAC71483.1; -; Genomic_DNA. DR PIR; I64228; I64228. DR RefSeq; WP_010869399.1; NC_000908.2. DR ProteinModelPortal; Q49406; -. DR EnsemblBacteria; AAC71483; AAC71483; MG_262. DR KEGG; mge:MG_262; -. DR PATRIC; 20010022; VBIMycGen98045_0303. DR KO; K02335; -. DR OMA; PEIIFEQ; -. DR OrthoDB; EOG6SJJH7; -. DR BioCyc; MGEN243273:GH2R-288-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1010; -; 1. 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; IPR008918; HhH2. DR InterPro; IPR029060; PIN_domain-like. DR Pfam; PF01367; 5_3_exonuc; 1. DR Pfam; PF02739; 5_3_exonuc_N; 1. DR SMART; SM00475; 53EXOc; 1. DR SMART; SM00279; HhH2; 1. DR SUPFAM; SSF47807; SSF47807; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 291 5'-3' exonuclease. FT /FTId=PRO_0000101286. SQ SEQUENCE 291 AA; 33271 MW; B026EFEFA1539CE7 CRC64; MKKAILIDGN SLAYRAYFAT WKQVEYAKQN NLPFNNAIRT MLLMCWNLIK ANVYQYGIVS FDTKAPTFRD QIYEGYKQKR VKTPVELLVQ IPLIKQALVY LGFLVCEKDG FEADDLIGSY ANLFTKQEIT VDIYSSDRDM LQLVNAFTNV FLCIKGTKEM VMYNNENFKS LFYGLAPYQV VEYKGLVGDN SDNLAGIKGI GPIKGIELLQ QYGTIDNIYT NFNNLPNQLQ KLLNNQKEIA KTFSFLAKIK TDIELDQNID LTGLKPIQKQ ALIQLLSENK INTLVEKFSK I // ID ESL3_MYCGE Reviewed; 273 AA. AC Q49421; Q49335; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Putative esterase/lipase 3; DE EC=3.1.-.-; GN OrderedLocusNames=MG344; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 193-255. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO 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; L43967; AAC71569.1; -; Genomic_DNA. DR EMBL; U02222; AAA03376.1; -; Genomic_DNA. DR PIR; A64238; A64238. DR RefSeq; WP_009885800.1; NZ_AAGX01000006.1. DR ProteinModelPortal; Q49421; -. DR STRING; 243273.MgenG_010200001828; -. DR ESTHER; mycge-esl3; AlphaBeta_hydrolase. DR EnsemblBacteria; AAC71569; AAC71569; MG_344. DR KEGG; mge:MG_344; -. DR PATRIC; 20010254; VBIMycGen98045_0404. DR eggNOG; ENOG41067V2; Bacteria. DR eggNOG; COG0596; LUCA. DR OMA; SAHIIYL; -. DR OrthoDB; EOG6PKFB7; -. DR BioCyc; MGEN243273:GH2R-394-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR Pfam; PF12697; Abhydrolase_6; 1. DR SUPFAM; SSF53474; SSF53474; 2. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome; Serine esterase. FT CHAIN 1 273 Putative esterase/lipase 3. FT /FTId=PRO_0000207078. FT ACT_SITE 34 34 {ECO:0000255}. FT ACT_SITE 100 100 Charge relay system. {ECO:0000250}. SQ SEQUENCE 273 AA; 31836 MW; C68C43B733F1F56C CRC64; MKRFSDLNQI DISKLEVFFQ PAKKTKKQTV VFAHGFSVFH SYFQSFYKTL TDYDYYAPLW PGHNVNGFDY KELSPIHYGE LLAAFIENKD LENIVLIGHS MGAAVCSYAM NLLNAKRVEK LILLAPLSYC NLLRYFKIKS SFKKDKAERM ANFKAMFQTK FSNLTDENSW ENELSKHSKM AKKLSNNILK ELPVLNKTYK NLKLPVFLVL AQNDLFMPTK LTLSYFNKYL IKNNNLQSSV ILNSEHQMFN SKYESFCKAM DDILNHNKLS KIY // ID FMT_MYCGE Reviewed; 311 AA. AC P47605; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Methionyl-tRNA formyltransferase; DE EC=2.1.2.9; GN Name=fmt; OrderedLocusNames=MG365; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71592.1; -; Genomic_DNA. DR PIR; D64240; D64240. DR RefSeq; WP_010869450.1; NC_000908.2. DR ProteinModelPortal; P47605; -. DR EnsemblBacteria; AAC71592; AAC71592; MG_365. DR KEGG; mge:MG_365; -. DR PATRIC; 20010312; VBIMycGen98045_0430. DR KO; K00604; -. DR OMA; KADIGIC; -. DR OrthoDB; EOG6B09WV; -. DR BioCyc; MGEN243273:GH2R-420-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.10.25.10; -; 1. DR Gene3D; 3.40.50.170; -; 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 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. PE 3: Inferred from homology; KW Complete proteome; Protein biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 311 Methionyl-tRNA formyltransferase. FT /FTId=PRO_0000082993. FT REGION 109 112 Tetrahydrofolate (THF) binding. FT {ECO:0000250}. SQ SEQUENCE 311 AA; 35536 MW; 38D96D99DCDC1EE0 CRC64; MFKIVFFGTS TLSKKCLEQL FYDNDFEICA VVTQPDKINH RNNKIVPSDV KSFCLEKNIT FFQPKQSISI KADLEKLKAD IGICVSFGQY LHQDIIDLFP NKVINLHPSK LPLLRGGAPL HWTIINGFKK SALSVIQLVK KMDAGPIWKQ QDFLVNNDWN TGDLSIYVEE HSPSFLIECT KEILNKKGKW FEQIGEPTFG LNIRKEQEHL DLNQIYKSFL NWVKGLAPKP GGWLSFEGKN IKIFKAKYVS KSNYKHQLGE IVNISRKGIN IALKSNEIIS IEKIQIPGKR VMEVSEIING KHPFVVGKCF K // ID FOLD_MYCGE Reviewed; 273 AA. AC P47259; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, 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}; OrderedLocusNames=MG013; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC71229.1; 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; L43967; AAC71229.1; ALT_INIT; Genomic_DNA. DR PIR; D64201; D64201. DR RefSeq; WP_009885972.1; NZ_AAGX01000015.1. DR ProteinModelPortal; P47259; -. DR STRING; 243273.MgenG_010200003146; -. DR EnsemblBacteria; AAC71229; AAC71229; MG_013. DR KEGG; mge:MG_013; -. DR PATRIC; 20009402; VBIMycGen98045_0013. DR eggNOG; ENOG4105CN0; Bacteria. DR eggNOG; COG0190; LUCA. DR KO; K01491; -. DR OMA; DIEGRHP; -. DR OrthoDB; EOG6K6VBB; -. DR BioCyc; MGEN243273:GH2R-13-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-HAMAP. 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: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; IPR020867; THF_DH/CycHdrlase_CS. 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. DR PROSITE; PS00766; THF_DHG_CYH_1; 1. DR PROSITE; PS00767; THF_DHG_CYH_2; 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 1 273 Bifunctional protein FolD. FT /FTId=PRO_0000199310. FT NP_BIND 149 151 NADP. {ECO:0000255|HAMAP-Rule:MF_01576}. FT BINDING 215 215 NADP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01576}. SQ SEQUENCE 273 AA; 30457 MW; 384F41EB94D0B3F2 CRC64; MSFDGKLKAQ SILETYKNFD WSKCKLVIIQ ANDDDSSDSF IKQKLIACNT VGAKSELIKL SNQITQAELI EKIISLNHDV NVTGIILQLP VYPHLDKNSL LEAINPLKDV DGLTTNHLAE IKPCIVEAII TLKELFNLEF NNQKIVVVGL GITGGKPIYE FLKTSGYKVQ ACDKDTPNTF ELIKSADIVF TAIGKSHFFQ AKNFKKGVIL FDIGVSRNKQ NKLCGDINPE GIEKKARWWT KTPGGVGPFT VLAIIKNLWI LHEKNKRCLQ SSI // ID FTSZ_MYCGE Reviewed; 369 AA. AC P47466; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909}; GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=MG224; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure CC in a strictly GTP-dependent manner. Interacts directly with CC several other division proteins. {ECO:0000255|HAMAP- CC Rule:MF_00909}. 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; L43967; AAC71445.1; -; Genomic_DNA. DR PIR; G64224; G64224. DR RefSeq; WP_010869382.1; NC_000908.2. DR ProteinModelPortal; P47466; -. DR EnsemblBacteria; AAC71445; AAC71445; MG_224. DR KEGG; mge:MG_224; -. DR PATRIC; 20009928; VBIMycGen98045_0260. DR KO; K03531; -. DR OMA; QNIDFED; -. DR OrthoDB; EOG6S7XZG; -. DR BioCyc; MGEN243273:GH2R-246-MONOMER; -. DR Proteomes; UP000000807; 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:0051301; P:cell division; IMP:CACAO. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-HAMAP. 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; IPR003008; Tubulin_FtsZ_GTPase. DR Pfam; PF00091; Tubulin; 1. DR PRINTS; PR00423; CELLDVISFTSZ. DR SMART; SM00864; Tubulin; 1. DR SUPFAM; SSF52490; SSF52490; 1. DR TIGRFAMs; TIGR00065; ftsZ; 1. DR PROSITE; PS01134; FTSZ_1; 1. DR PROSITE; PS01135; FTSZ_2; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; Cytoplasm; GTP-binding; KW Nucleotide-binding; Reference proteome; Septation. FT CHAIN 1 369 Cell division protein FtsZ. FT /FTId=PRO_0000114360. FT NP_BIND 27 31 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT NP_BIND 119 121 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 150 150 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 189 189 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. SQ SEQUENCE 369 AA; 41604 MW; 6173D93AA0FCF5A0 CRC64; MDENETQFNK LNQVKNKLKI GVFGIGGAGN NIVDASLYHY PNLASENIHF YAINSDLQHL AFKTNVKNKL LIQDHTNKGF GAGGDPAKGA SLAISFQEQF NTLTDGYDFC ILVAGFGKGT GTGATPVFSK ILKTKKILNV AIVTYPSLNE GLTVRNKATK GLEILNKATD SYMLFCNEKC TNGIYQLANT EIVSAIKNLI ELITIPLQQN IDFEDVRAFF QTKKTNQDQQ LFTVTHPFSF SFDSKDSIEQ FAKQFKNFEK VSYFDHSIVG AKKVLLKANI NQKIVKLNFK QIQDIIWTKI DNYQLEIRLG VDFVTTIPNI QIFILSEHKN PVSLPIDNKS TENNQNKLKL LDELKELGMK YVKHQNQIY // ID FRUK_MYCGE Reviewed; 300 AA. AC Q49396; Q49226; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 83. DE RecName: Full=Putative 1-phosphofructokinase; DE EC=2.7.1.56; DE AltName: Full=Fructose 1-phosphate kinase; GN Name=fruK; OrderedLocusNames=MG063; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-253. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 1-phosphate = ADP + D- CC fructose 1,6-bisphosphate. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC71280.1; 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; L43967; AAC71280.1; ALT_INIT; Genomic_DNA. DR EMBL; U01777; AAD10597.1; -; Genomic_DNA. DR ProteinModelPortal; Q49396; -. DR EnsemblBacteria; AAC71280; AAC71280; MG_063. DR KEGG; mge:MG_063; -. DR PATRIC; 20009510; VBIMycGen98045_0064. DR KO; K00882; -. DR OMA; PAIDMNV; -. DR OrthoDB; EOG61KBKF; -. DR BioCyc; MGEN243273:GH2R-66-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 300 Putative 1-phosphofructokinase. FT /FTId=PRO_0000080068. SQ SEQUENCE 300 AA; 33521 MW; 7C979CAE5DFEB795 CRC64; MQNITKESKI WIVNYACAID YYVDLNKQKN SVLIPGGKGI NVAIVMKSLG FDPTVITFLG QPTKNLFLEL VKPYDLNIVS FISETKTRIN LKLLKDEKTT EINDLSPLIT DANLTELLTF LKANVKNNDL VIINGRFKFE ALEKVLNLVF TLTENVVIDV DESKMLTLLN QSKPLVMKPN IDEFQTMINT FFHDQQSLIA AIKKFHYCKL LLLSDGDKGA YLFDQNKLLF VSSITPKQVV STTGAGDTLL AVFLANLILK VDLKTALIKA TNYASATISK LGVVDSKDKI SVITPKSYYL // ID FTSH_MYCGE Reviewed; 702 AA. AC P47695; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 117. 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}; OrderedLocusNames=MG457; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01458}. CC -!- SUBCELLULAR LOCATION: Cell 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; L43967; AAC72477.1; -; Genomic_DNA. DR PIR; E64250; E64250. DR RefSeq; WP_009885575.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47695; -. DR SMR; P47695; 228-467. DR STRING; 243273.MgenG_010200000145; -. DR MEROPS; M41.009; -. DR PRIDE; P47695; -. DR EnsemblBacteria; AAC72477; AAC72477; MG_457. DR KEGG; mge:MG_457; -. DR PATRIC; 20010506; VBIMycGen98045_0526. DR eggNOG; ENOG4105C3H; Bacteria. DR eggNOG; COG0465; LUCA. DR KO; K03798; -. DR OMA; HTEAWTI; -. DR OrthoDB; EOG6PKFBJ; -. DR BioCyc; MGEN243273:GH2R-510-MONOMER; -. DR Proteomes; UP000000807; 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-HAMAP. DR GO; GO:0016887; F:ATPase 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:0030163; P:protein catabolic process; IEA:UniProtKB-HAMAP. 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; IPR000642; Peptidase_M41. DR Pfam; PF00004; AAA; 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 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Metal-binding; Metalloprotease; Nucleotide-binding; Protease; KW Reference proteome; Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1 702 ATP-dependent zinc metalloprotease FtsH. FT /FTId=PRO_0000084639. FT TOPO_DOM 1 26 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TRANSMEM 27 47 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TOPO_DOM 48 175 Extracellular. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TRANSMEM 176 196 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TOPO_DOM 197 702 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT NP_BIND 271 278 ATP. {ECO:0000255|HAMAP-Rule:MF_01458}. FT ACT_SITE 494 494 {ECO:0000255|HAMAP-Rule:MF_01458}. FT METAL 493 493 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT METAL 497 497 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT METAL 572 572 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. SQ SEQUENCE 702 AA; 76730 MW; ADB26C68CD780535 CRC64; MKKRNKGLVE QTTTEKNNFS RKTAWKVFWW VIILAVVIGV LAYIFSPRAA TAVVESWKLN GGSNSTLTAK VSGFSNELTF KQINGSTYVT DTILQVSITF DGLNSPLTVT AHKTVNSNGN VIFNIANLSI NQSNGQITVN SNGTMMNGGS SNNTKSIAGF ETLGTFIAPD TRARDVLNGL FGLLPIIIFV VFFLLFWRSA RGISAGGREE DNIFSIGKTQ AKLAKSTVKF TNIAGLQEEK HELLEIVDYL KNPLKYAQMG ARSPRGVILY GPPGTGKTLL AKAVAGEAGV PFFQSTGSGF EDMLVGVGAK RVRDLFNKAK KAAPCIIFID EIDSVGSKRG RVELSSYSVV EQTLNQLLAE MDGFTSRTGV VVMAATNRLD VLDDALLRPG RFDRHIQINL PDIKEREGIL KVHAENKNLS SKISLLDVAK RTPGFSGAQL ENVINEATLL AVRDNRTTIN INDIDEAIDR VIAGPAKKSR VISDEDRKLV AYHEAGHALV GLHVHSNDEV QKITIIPRGQ AGGYTLSTPK SGDLNLKRKS DLLAMIATAM GGRAAEEEIY GNLEITTGAS SDFYKATNIA RAMVTQLGMS KLGQVQYVPS QGTLPSNVKL YSEQTAKDID NEINFIIEEQ YKKAKTIIKS NRKELELLVE ALLIAETILK SDIDFIHKNT KLPPEILLQK QEQQAKQKLN KSEVKPESET NS // ID G3P_MYCGE Reviewed; 337 AA. AC P47543; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 113. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P9WN83}; DE Short=GAPDH {ECO:0000250|UniProtKB:P9WN83}; DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P9WN83}; DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P9WN83}; GN Name=gapA; Synonyms=gap; OrderedLocusNames=MG301; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81 AND 279-337. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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:P9WN83}. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC {ECO:0000250|UniProtKB:P9WN83}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P54226}. 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; L43967; AAC71523.1; -; Genomic_DNA. DR EMBL; U02213; AAD12507.1; -; Genomic_DNA. DR EMBL; U02178; AAD12463.1; -; Genomic_DNA. DR PIR; C64233; C64233. DR RefSeq; WP_009885879.1; NZ_AAGX01000008.1. DR ProteinModelPortal; P47543; -. DR SMR; P47543; 9-337. DR STRING; 243273.MgenG_010200002484; -. DR PRIDE; P47543; -. DR EnsemblBacteria; AAC71523; AAC71523; MG_301. DR KEGG; mge:MG_301; -. DR PATRIC; 20010132; VBIMycGen98045_0352. DR eggNOG; ENOG4105C17; Bacteria. DR eggNOG; COG0057; LUCA. DR KO; K00134; -. DR OMA; TFDHEVS; -. DR OrthoDB; EOG66TG3S; -. DR BioCyc; MGEN243273:GH2R-337-MONOMER; -. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycolysis; NAD; Nucleotide-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 337 Glyceraldehyde-3-phosphate dehydrogenase. FT /FTId=PRO_0000145668. FT NP_BIND 17 18 NAD. {ECO:0000250|UniProtKB:P00362}. FT REGION 156 158 Glyceraldehyde 3-phosphate binding. FT {ECO:0000250|UniProtKB:P00362}. FT REGION 215 216 Glyceraldehyde 3-phosphate binding. FT {ECO:0000250|UniProtKB:P00362}. FT ACT_SITE 157 157 Nucleophile. FT {ECO:0000250|UniProtKB:P00362}. FT BINDING 39 39 NAD. {ECO:0000250|UniProtKB:P00362}. FT BINDING 83 83 NAD; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:P00362}. FT BINDING 125 125 NAD. {ECO:0000250|UniProtKB:P00362}. FT BINDING 187 187 Glyceraldehyde 3-phosphate. FT {ECO:0000250|UniProtKB:P00362}. FT BINDING 202 202 Glyceraldehyde 3-phosphate. FT {ECO:0000250|UniProtKB:P00362}. FT BINDING 238 238 Glyceraldehyde 3-phosphate. FT {ECO:0000250|UniProtKB:P00362}. FT BINDING 319 319 NAD. {ECO:0000250|UniProtKB:P00362}. FT SITE 184 184 Activates thiol group during catalysis. FT {ECO:0000250|UniProtKB:P00362}. SQ SEQUENCE 337 AA; 37098 MW; FA1EA1966687006B CRC64; MAAKNRTIKV AINGFGRIGR LVFRSLLSKA NVEVVAINDL TQPEVLAHLL KYDSAHGELK RKITVKQNIL QIDRKKVYVF SEKDPQNLPW DEHDIDVVIE STGRFVSEEG ASLHLKAGAK RVIISAPAKE KTIRTVVYNV NHKTISSDDK IISAASCTTN CLAPLVHVLE KNFGIVYGTM LTVHAYTADQ RLQDAPHNDL RRARAAAVNI VPTTTGAAKA IGLVVPEANG KLNGMSLRVP VLTGSIVELS VVLEKSPSVE QVNQAMKRFA SASFKYCEDP IVSSDVVSSE YGSIFDSKLT NIVEVDGMKL YKVYAWYDNE SSYVHQLVRV VSYCAKL // ID FTSY_MYCGE Reviewed; 346 AA. AC P47539; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000255|HAMAP-Rule:MF_00920}; DE Short=SRP receptor {ECO:0000255|HAMAP-Rule:MF_00920}; GN Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920}; OrderedLocusNames=MG297; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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:0000255|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:0000255|HAMAP-Rule:MF_00920}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00920}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily. CC {ECO:0000255|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; L43967; AAC71519.1; -; Genomic_DNA. DR EMBL; U02177; AAD12462.1; -; Genomic_DNA. DR PIR; H64232; H64232. DR RefSeq; WP_009885877.1; NZ_AAGX01000008.1. DR ProteinModelPortal; P47539; -. DR STRING; 243273.MgenG_010200002454; -. DR EnsemblBacteria; AAC71519; AAC71519; MG_297. DR KEGG; mge:MG_297; -. DR PATRIC; 20010124; VBIMycGen98045_0348. DR eggNOG; ENOG4105CCP; Bacteria. DR eggNOG; COG0552; LUCA. DR KO; K03110; -. DR OMA; VRNENIE; -. DR OrthoDB; EOG62K1ZH; -. DR BioCyc; MGEN243273:GH2R-333-MONOMER; -. DR Proteomes; UP000000807; 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: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 3: Inferred from homology; KW Cell membrane; Complete proteome; Cytoplasm; GTP-binding; Membrane; KW Nucleotide-binding; Receptor; Reference proteome. FT CHAIN 1 346 Signal recognition particle receptor FT FtsY. FT /FTId=PRO_0000101135. FT NP_BIND 143 150 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. FT NP_BIND 225 229 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. FT NP_BIND 289 292 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. SQ SEQUENCE 346 AA; 38859 MW; 241664C8588D0B07 CRC64; MGFLSKLIAK LKPKKSVAKQ LKEEVEKQSL FQTNNKTYYQ GLKKSATTFA KTINELSKRY VNVDEQFKEN LFEGLVLLDV GYHAANKICD AIIEQIKLNR ITDFQLIKEL IIDQIIVYYI QDKLFDTDLI VKPNFTNVYL FVGVNGVGKT TTLAKIADFF IKQNKRVLLV AGDTFRAGAI EQLNQWAKLL NCDIVLPNPK EQTPAVIFRG VKKGIDDKYD FVLCDTSGRL QNKLNLMNEL QKIYQIIQKV SGSEPSETLL VLDGTVGQTG LSQAKVFNEF SKLTGIVLTK MDGSAKGGII LAIKDMFNLP VKLIGFGEKT SDLAIFDLEK YVLGLLNNLN LDNKEN // ID GALE_MYCGE Reviewed; 340 AA. AC P47364; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=UDP-glucose 4-epimerase; DE EC=5.1.3.2; DE AltName: Full=Galactowaldenase; DE AltName: Full=UDP-galactose 4-epimerase; GN Name=galE; OrderedLocusNames=MG118; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Involved in the metabolism of galactose. Catalyzes the CC conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) CC through a mechanism involving the transient reduction of NAD (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose = UDP-alpha-D-galactose. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase 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; L43967; AAC71336.1; -; Genomic_DNA. DR PIR; A64213; A64213. DR RefSeq; WP_010869340.1; NC_000908.2. DR ProteinModelPortal; P47364; -. DR EnsemblBacteria; AAC71336; AAC71336; MG_118. DR KEGG; mge:MG_118; -. DR PATRIC; 20009640; VBIMycGen98045_0129. DR KO; K01784; -. DR OMA; RWGPFVQ; -. DR OrthoDB; EOG6WHNS9; -. DR BioCyc; MGEN243273:GH2R-122-MONOMER; -. DR UniPathway; UPA00214; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR005886; GalE. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF16363; GDP_Man_Dehyd; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01179; galE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Galactose metabolism; KW Isomerase; NAD; Reference proteome. FT CHAIN 1 340 UDP-glucose 4-epimerase. FT /FTId=PRO_0000183209. FT NP_BIND 16 17 NAD. {ECO:0000250}. FT NP_BIND 37 42 NAD. {ECO:0000250}. FT NP_BIND 60 61 NAD. {ECO:0000250}. FT NP_BIND 82 86 NAD. {ECO:0000250}. FT REGION 199 200 Substrate binding. {ECO:0000250}. FT REGION 216 218 Substrate binding. {ECO:0000250}. FT REGION 295 298 Substrate binding. {ECO:0000250}. FT ACT_SITE 154 154 Proton acceptor. {ECO:0000250}. FT BINDING 127 127 NAD. {ECO:0000250}. FT BINDING 127 127 Substrate. {ECO:0000250}. FT BINDING 154 154 NAD. {ECO:0000250}. FT BINDING 154 154 Substrate. {ECO:0000250}. FT BINDING 158 158 NAD. {ECO:0000250}. FT BINDING 182 182 NAD; via carbonyl oxygen. {ECO:0000250}. FT BINDING 183 183 Substrate. {ECO:0000250}. FT BINDING 231 231 Substrate. {ECO:0000250}. SQ SEQUENCE 340 AA; 38425 MW; 98261DC92DB1C0EE CRC64; MIGAKTRVAI VGGIGYIGSC FASFIKEQND KLIVTVIDNN KNNHVIKLLK KIGIEFYFAD LLDRHKLTEV IAAIQPDVVF HFAAKTSVSE SVHNPLKYFD CNVIGTLNLI SAISNLQKPI KLFFASSAAV YGQTTNSYIS EEIVITETQA TNPYGLSKFL DELILNAVAK NSQLQVVCLR FFNVAGAILP FGNFNGNTTL LIPNLVKAFL KQTPFFLYGN DYATKDGSCI RDYIHVYDIC NAHFLLWKWL NDHRQIKFET FNLGSGIGTS NLEVIDIAKK VFYPSRLNLE IRPKRSWDPA ILVANVAKAK QTFQFKITRN LKDMISDERN FYENFYNDAY // ID FPG_MYCGE Reviewed; 284 AA. AC P55825; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-MAY-2016, entry version 117. DE RecName: Full=Formamidopyrimidine-DNA glycosylase; DE Short=Fapy-DNA glycosylase; DE EC=3.2.2.23; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM; DE Short=AP lyase MutM; DE EC=4.2.99.18; GN Name=mutM; Synonyms=fpg; OrderedLocusNames=MG262.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RX PubMed=8638118; DOI=10.1126/science.271.5253.1302b; RA Robison K., Gilbert W., Church G.M.; RT "More Haemophilus and Mycoplasma genes."; RL Science 271:1302-1303(1996). CC -!- FUNCTION: Involved in base excision repair of DNA damaged by CC oxidation or by mutagenic agents. Acts as DNA glycosylase that CC recognizes and removes damaged bases. Has a preference for CC oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has CC AP (apurinic/apyrimidinic) lyase activity and introduces nicks in CC the DNA strand. Cleaves the DNA backbone by beta-delta elimination CC to generate a single-strand break at the site of the removed base CC with both 3'- and 5'-phosphates (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7- CC methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N- CC methyl)formamidopyrimidine. 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 -!- 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 -!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FPG-type zinc finger. {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; L43967; AAC71484.1; -; Genomic_DNA. DR RefSeq; WP_010869400.1; NC_000908.2. DR ProteinModelPortal; P55825; -. DR EnsemblBacteria; AAC71484; AAC71484; MG_498. DR KEGG; mge:MG_498; -. DR PATRIC; 20010024; VBIMycGen98045_0304. DR KO; K10563; -. DR OMA; VCQPRPR; -. DR OrthoDB; EOG6QP131; -. DR BioCyc; MGEN243273:GH2R-289-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro. DR HAMAP; MF_00103; Fapy_DNA_glycosyl; 1. DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd. DR InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS. DR InterPro; IPR020629; Formamido-pyr_DNA_Glyclase. DR InterPro; IPR012319; FPG_cat. DR InterPro; IPR010979; Ribosomal_S13-like_H2TH. DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase. DR InterPro; IPR010663; Znf_FPG/IleRS. DR Pfam; PF01149; Fapy_DNA_glyco; 1. DR Pfam; PF06831; H2TH; 1. DR Pfam; PF06827; zf-FPG_IleRS; 1. DR SMART; SM00898; Fapy_DNA_glyco; 1. DR SMART; SM01232; H2TH; 1. DR SUPFAM; SSF46946; SSF46946; 1. DR SUPFAM; SSF81624; SSF81624; 1. DR TIGRFAMs; TIGR00577; fpg; 1. DR PROSITE; PS51068; FPG_CAT; 1. DR PROSITE; PS01242; ZF_FPG_1; 1. DR PROSITE; PS51066; ZF_FPG_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosidase; KW Hydrolase; Lyase; Metal-binding; Multifunctional enzyme; KW Reference proteome; Zinc; Zinc-finger. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 284 Formamidopyrimidine-DNA glycosylase. FT /FTId=PRO_0000170836. FT ZN_FING 239 273 FPG-type. FT ACT_SITE 2 2 Schiff-base intermediate with DNA. FT {ECO:0000250}. FT ACT_SITE 3 3 Proton donor. {ECO:0000250}. FT ACT_SITE 59 59 Proton donor; for beta-elimination FT activity. {ECO:0000250}. FT ACT_SITE 263 263 Proton donor; for delta-elimination FT activity. {ECO:0000250}. FT BINDING 94 94 DNA. {ECO:0000250}. FT BINDING 113 113 DNA. {ECO:0000250}. SQ SEQUENCE 284 AA; 32749 MW; 0D04A1F6082FF2FC CRC64; MPELPEVTTV INELKETVLN KPLDQVQVNL RKVLKNIDPQ LLNKQLKNQF FTDIKRKGKY IIFLLSNGLY LVSHLRMEGK YFFEERGSKF NQKHVLVEFH FDDGSQLNYH DTRQFGTFHL YEKLEQAAQL NKLAFDPLEA GFDYRKIFQK AQNSKRKVKT FILDQTVISG IGNIYADEIL FASKINPETM VDQLTIKEIE ILCKNATKIL AKAIVMKGTT ISSFSFKKDH TGGYQNFLKV HTKKDQPCSV CNQLIVKKKI NGRGSYFCLN CQKITTKVST KLNP // ID GATA_MYCGE Reviewed; 477 AA. AC P47345; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 90. 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=MG099; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71317.1; -; Genomic_DNA. DR PIR; I64210; I64210. DR RefSeq; WP_010869331.1; NC_000908.2. DR ProteinModelPortal; P47345; -. DR STRING; 243273.MgenG_010200000730; -. DR EnsemblBacteria; AAC71317; AAC71317; MG_099. DR KEGG; mge:MG_099; -. DR PATRIC; 20009600; VBIMycGen98045_0109. DR eggNOG; ENOG4107U77; Bacteria. DR eggNOG; COG0154; LUCA. DR KO; K02433; -. DR OMA; TVARWIE; -. DR OrthoDB; EOG61P6R9; -. DR BioCyc; MGEN243273:GH2R-102-MONOMER; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 477 Glutamyl-tRNA(Gln) amidotransferase FT subunit A. FT /FTId=PRO_0000105178. FT ACT_SITE 68 68 Charge relay system. {ECO:0000250}. FT ACT_SITE 143 143 Charge relay system. {ECO:0000250}. FT ACT_SITE 167 167 Acyl-ester intermediate. {ECO:0000250}. SQ SEQUENCE 477 AA; 53408 MW; 0D4A99D75C3DBF2B CRC64; MRSNILSLRA ILDKKPSAIN DVLTSINAKI ELNKSSNFLL KNTVEIYSKK INKSDEKILL NNIPYVLKDN IATKDIVTTG GSLFLKNYLP PFSATVFELL EMNGALLVGK ANMDEFGLGG TGSYSAFGVV HHPENSSLIA GGSSSGSAYA VAKDIVPFSI ATDTGDSIRR PASICNVVGF KPTYGLISRN GVFPYAPSMD HVGIFAKFVS DIAIVSDVVI KHDKTDFSSQ KSPDENQFFN ELAIPFTRSI RFGYLKPLEK LFNKHLQKKW NNLKKTLEQK NYQLIPLDFD VELLKVIDSI YKIISYSEAV SCYSNLTGIV FGQKVFEPNS PSNFDQTITR NRDQFLGKQL KRRFVIGAFA TDEKNFEKYF EKAQKIRRVL VDNFLNLFSD VDFVLSPSAS CFASTIEDIQ ANKPYTNIID DFLQLANFAG SPSITIPWLV QTKDQTIGLS ISANCFEDKK LLQIAYWFEQ LFDLNHD // ID G6PI_MYCGE Reviewed; 431 AA. AC P47357; Q49449; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2001, sequence version 2. DT 13-APR-2016, entry version 98. 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=MG111; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC71329.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAD10560.1; 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; L43967; AAC71329.1; ALT_INIT; Genomic_DNA. DR EMBL; U01747; AAD10560.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_010869336.1; NC_000908.2. DR ProteinModelPortal; P47357; -. DR EnsemblBacteria; AAC71329; AAC71329; MG_111. DR KEGG; mge:MG_111; -. DR PATRIC; 20009626; VBIMycGen98045_0122. DR KO; K01810; -. DR OMA; FGYFYFW; -. DR OrthoDB; EOG64R61J; -. DR BioCyc; MGEN243273:GH2R-115-MONOMER; -. DR UniPathway; UPA00109; UER00181. DR Proteomes; UP000000807; 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 HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. DR InterPro; IPR018189; Phosphoglucose_isomerase_CS. DR PANTHER; PTHR11469; PTHR11469; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; KW Reference proteome. FT CHAIN 1 431 Glucose-6-phosphate isomerase. FT /FTId=PRO_0000180679. FT ACT_SITE 284 284 Proton donor. {ECO:0000250}. FT ACT_SITE 305 305 {ECO:0000250}. FT ACT_SITE 420 420 {ECO:0000250}. SQ SEQUENCE 431 AA; 49253 MW; BDAFD77342B3B4F5 CRC64; MSDKLLTIDL SHVYGFDKEI IFKKYQKKVD QIHQDFLAHK LADGHMTGWY DQPDQNHQFL LKTINQIDKK FKSLKVTDIV YVGIGGSFTG IKTVLDFLKP KQRTGLKIHF VPDLSAFQAA SVIKEIKNKS WALITTSKSG RTLEPALNFR IFRNLLNKRY GNKHYQRVVV ITDEKKGLLT KMASNHGYQK LVIDSNIGGR FSTLSPAGLL LAKLFGHDPK AILKGTLQAK KDLQTTSLEN NSAYLYAVVR HWLYTTKKFK IEVCIAYHSL YEYLLLQHRQ LFGESEGKND KSLFPTFSIF TVDLHSMGQL YQEGEKVFFE TVIDVKNPLV NINLPPSDFD NDDELDFLLD KSLNEISDVA IDSVIKAHYQ ANVSIIKLTL KEQSAFMFGY FYFWLSVATV MSGSLLGHNV FNQPGVEVYK KLMFEKLRSG H // ID GLF_MYCGE Reviewed; 404 AA. AC Q49398; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=UDP-galactopyranose mutase; DE Short=UGM; DE EC=5.4.99.9; DE AltName: Full=UDP-GALP mutase; DE AltName: Full=Uridine 5-diphosphate galactopyranose mutase; GN Name=glf; OrderedLocusNames=MG137; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Involved in the conversion of UDP-GalP into UDP-GalF CC through a 2-keto intermediate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UDP-alpha-D-galactopyranose = UDP-alpha-D- CC galactofuranose. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the UDP-galactopyranose/dTDP-fucopyranose CC mutase 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; L43967; AAC71354.1; -; Genomic_DNA. DR PIR; B64215; B64215. DR ProteinModelPortal; Q49398; -. DR STRING; 243273.MgenG_010200000960; -. DR EnsemblBacteria; AAC71354; AAC71354; MG_137. DR KEGG; mge:MG_137; -. DR PATRIC; 20009680; VBIMycGen98045_0149. DR eggNOG; ENOG4107R6R; Bacteria. DR eggNOG; COG0562; LUCA. DR KO; K01854; -. DR OMA; MPENGYT; -. DR OrthoDB; EOG62K1X2; -. DR BioCyc; MGEN243273:GH2R-141-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0008767; F:UDP-galactopyranose mutase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.720; -; 3. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR004379; UDP-GALP_mutase. DR InterPro; IPR015899; UDP-GalPyranose_mutase_C. DR PANTHER; PTHR21197; PTHR21197; 1. DR Pfam; PF03275; GLF; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR TIGRFAMs; TIGR00031; UDP-GALP_mutase; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Isomerase; Reference proteome. FT CHAIN 1 404 UDP-galactopyranose mutase. FT /FTId=PRO_0000087509. FT NP_BIND 50 51 FAD. {ECO:0000250}. FT NP_BIND 77 78 FAD. {ECO:0000250}. FT NP_BIND 386 391 FAD. {ECO:0000250}. FT BINDING 31 31 FAD. {ECO:0000250}. FT BINDING 58 58 FAD; via amide nitrogen. {ECO:0000250}. FT BINDING 176 176 UDP-GalP. {ECO:0000250}. FT BINDING 180 180 UDP-GalP. {ECO:0000250}. FT BINDING 205 205 UDP-GalP. {ECO:0000250}. FT BINDING 302 302 UDP-GalP. {ECO:0000250}. FT BINDING 311 311 UDP-GalP. {ECO:0000250}. FT BINDING 350 350 UDP-GalP. {ECO:0000250}. FT BINDING 379 379 FAD. {ECO:0000250}. FT BINDING 385 385 UDP-GalP. {ECO:0000250}. SQ SEQUENCE 404 AA; 46661 MW; 67B8DAB814A3A680 CRC64; MNVILSVMLF SSPSCVNINS FDILIVGAGI SGIVLANILA NHNKRVLIVE KRDHIGGNCY DKVDSKTQLL FHQYGPHIFH TNNQTVINFI SPFFELNNYH HRVGLKLKNN LDLTLPFDFQ QIYKLMGKDG RKLVSFFKEN FSLNTHLSLA ELQLIDNPLA QKLYQFLISN VYKPYSVKMW GLPFAMINEN VINRVKIVLS EQSSYFPDAI IQGLPKSGYT NSFLKMLANP LIDVQLNCKD NLLVYQDEKL FFNNNLIEKP VVYCGLIDKL FNFCFGHLQY RSLAFSWKRF NQKKYQTYPV VNMPLAKSIT RSVEYKQLTN QGSFKPQTIV SFETPGSYAI NDPRFNEPYY PINNTLNDTL FKKYWKKASK LKNLHLLGRL ATYQYIDMDK AILLSIKKAQ QLLS // ID GALU_MYCGE Reviewed; 292 AA. AC P47691; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase; DE EC=2.7.7.9; DE AltName: Full=Alpha-D-glucosyl-1-phosphate uridylyltransferase; DE AltName: Full=UDP-glucose pyrophosphorylase; DE Short=UDPGP; DE AltName: Full=Uridine diphosphoglucose pyrophosphorylase; GN Name=galU; Synonyms=gtaB; OrderedLocusNames=MG453; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-163. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: May play a role in stationary phase survival. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UTP + alpha-D-glucose 1-phosphate = CC diphosphate + UDP-glucose. CC -!- SIMILARITY: Belongs to the UDPGP type 2 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; L43967; AAC72473.1; -; Genomic_DNA. DR EMBL; U02258; AAD12523.1; -; Genomic_DNA. DR PIR; A64250; A64250. DR RefSeq; WP_009885581.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47691; -. DR STRING; 243273.MgenG_010200000175; -. DR EnsemblBacteria; AAC72473; AAC72473; MG_453. DR KEGG; mge:MG_453; -. DR PATRIC; 20010496; VBIMycGen98045_0521. DR eggNOG; ENOG4107XYG; Bacteria. DR eggNOG; COG1210; LUCA. DR KO; K00963; -. DR OMA; VALMEVE; -. DR OrthoDB; EOG6Z9B3V; -. DR BioCyc; MGEN243273:GH2R-506-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR005771; GalU_uridylyltTrfase_bac/arc. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR01099; galU; 1. PE 3: Inferred from homology; KW Complete proteome; Nucleotidyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 292 UTP--glucose-1-phosphate FT uridylyltransferase. FT /FTId=PRO_0000201359. SQ SEQUENCE 292 AA; 32514 MW; 27EB08EC8147E93A CRC64; MKTKIRKAVI PAAGLGVRLL PATKAIPKEM LPLVNKPTIQ YIVEEAVKSG IEQILVIVSS KKTAILDHFD YDLILENALI QKNKLQEHKE IEDIANLAHI FFVRQKNQDG LGDAILFAES FVGNEDFAVL LGDDVVFSKE PALKQCLEAY YETNCQTIGV QEVDPCHVDK YGIITPEGDY KNKDLIKVLA MTEKPKPKDA KSNLAILGRY VLKPSIFKAL RSVPYGVGGE LQLTDGLNFC LKNENFYARK FTGTRFDVGT KSGFIKANLF TALNNKDISK KEVLELLNLV KA // ID GATB_MYCGE Reviewed; 477 AA. AC P47346; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 94. 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=MG100; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 80-177. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71318.1; -; Genomic_DNA. DR EMBL; U01799; AAD12325.1; -; Genomic_DNA. DR PIR; A64211; A64211. DR RefSeq; WP_009885658.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47346; -. DR STRING; 243273.MgenG_010200000735; -. DR PRIDE; P47346; -. DR EnsemblBacteria; AAC71318; AAC71318; MG_100. DR KEGG; mge:MG_100; -. DR PATRIC; 20009602; VBIMycGen98045_0110. DR eggNOG; ENOG4105CHT; Bacteria. DR eggNOG; COG0064; LUCA. DR KO; K02434; -. DR OMA; CQLAIAN; -. DR OrthoDB; EOG6RJV5B; -. DR BioCyc; MGEN243273:GH2R-103-MONOMER; -. DR Proteomes; UP000000807; 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 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 477 Aspartyl/glutamyl-tRNA(Asn/Gln) FT amidotransferase subunit B. FT /FTId=PRO_0000148807. SQ SEQUENCE 477 AA; 54695 MW; E8A05FA097913D96 CRC64; MINFEAIIGI EVHVVLNTAS KMFSKAPNRV DNQKINHFID PIDLGLPGTL PQVNELAVYK ALLLADALKM KTVTNKLVFD RKHYFYQDLP KGFQITQQNY PFAKNGVVTI NVDAIEKPIY IDRFHLEEDT AKQHFNHDQI LLDFNRCGAP LIEVVTLPVI NTAKEAKAYL QKLRQILIVN NISNAKLEDG SMRSDCNVSV RLKGQRQLGT KIEIKNINSL NNVEKAIDLE INRQVKALIN GETLSQATLS FDDKTNNNVF MRKKDNTIDY RYFIEPNIMT SNIDDLLLEK PVAFQLEQFQ KELIDSNVNP QLVQLVVDDA TIFSAFQTIN SVIKNPQETI RWLCIELIGQ LNKTNSSLTA NLIQDLITLI EMLKAAKVNQ KQAKQLITLM IETKKDPKSL AKLHNLEQIT DPKELQKIIK KIFQENEKEI LKNIDRIERI QKLIIGQVMH KTNNRANPQQ VFIIVENMLH EVRERDS // ID GLPK_MYCGE Reviewed; 508 AA. AC P47284; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=Glycerol kinase {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 {ECO:0000255|HAMAP-Rule:MF_00186}; DE AltName: Full=Glycerokinase {ECO:0000255|HAMAP-Rule:MF_00186}; DE Short=GK {ECO:0000255|HAMAP-Rule:MF_00186}; GN Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186}; OrderedLocusNames=MG038; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71254.1; -; Genomic_DNA. DR PIR; B64204; B64204. DR RefSeq; WP_010869300.1; NC_000908.2. DR ProteinModelPortal; P47284; -. DR EnsemblBacteria; AAC71254; AAC71254; MG_038. DR KEGG; mge:MG_038; -. DR PATRIC; 20009452; VBIMycGen98045_0036. DR KO; K00864; -. DR OMA; GWVEHEP; -. DR OrthoDB; EOG6RZB46; -. DR BioCyc; MGEN243273:GH2R-38-MONOMER; -. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB. 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 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 1 508 Glycerol kinase. FT /FTId=PRO_0000059467. FT NP_BIND 15 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT NP_BIND 419 423 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT REGION 85 86 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT REGION 251 252 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 15 15 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 19 19 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 138 138 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 273 273 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 317 317 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 336 336 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. SQ SEQUENCE 508 AA; 56902 MW; 82033D7076D27CB5 CRC64; MDLKKQYIIA LDEGTSSCRS IVFDHNLNQI AIAQNEFNTF FPNSGWVEQD PLEIWSAQLA TMQSAKNKAQ IKSHEVIAVG ITNQRETIVL WNKENGLPVY NAIVWQDQRT AALCQKFNED KLIQTKVKQK TGLPINPYFS ATKIAWILKN VPLAKKLMEQ KKLLFGTIDS WLIWKLTNGK MHVTDVSNAS RTLLFDIVKM EWSKELCDLF EVPVSILPKV LSSNAYFGDI ETNHWSSNAK GIVPIRAVLG DQQAALFGQL CTEPGMVKNT YGTGCFVLMN IGDKPTLSKH NLLTTVAWQL ENHPPVYALE GSVFVAGAAI KWLRDALKII YSEKESDFYA ELAKENEQNL VFVPAFSGLG APWWDASARG IILGIEASTK REHIVKASLE SIAFQTNDLL NAMASDLGYK ITSIKADGGI VKSNYLMQFQ ADIADVIVSI PKNKETTAVG VCFLAGLACG FWKDIHQLEK LTTLDKKFKS TMDPNIRKTK INSWHKAVER ALKWKEID // ID GLPF_MYCGE Reviewed; 258 AA. AC P47279; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 100. DE RecName: Full=Probable glycerol uptake facilitator protein; GN Name=glpF; OrderedLocusNames=MG033; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71249.1; -; Genomic_DNA. DR RefSeq; WP_009885697.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47279; -. DR STRING; 243273.MgenG_010200000990; -. DR EnsemblBacteria; AAC71249; AAC71249; MG_033. DR KEGG; mge:MG_033; -. DR PATRIC; 20009442; VBIMycGen98045_0031. DR eggNOG; ENOG4107R3W; Bacteria. DR eggNOG; COG0580; LUCA. DR KO; K02440; -. DR OMA; KIFTWLA; -. DR OrthoDB; EOG6P8TRZ; -. DR BioCyc; MGEN243273:GH2R-33-MONOMER; -. DR Proteomes; UP000000807; 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:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. 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 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 1 258 Probable glycerol uptake facilitator FT protein. FT /FTId=PRO_0000064087. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 50 70 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 152 172 Helical. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. FT TRANSMEM 233 253 Helical. {ECO:0000255}. FT MOTIF 77 79 NPA 1. FT MOTIF 206 208 NPA 2. SQ SEQUENCE 258 AA; 27667 MW; 238DBE6ABA4E1438 CRC64; MYFQNSTQLG WWFLAELIGT FILIIFGNGA VAQVNLKKMA TSETKAKFLT VALTWGIGVL FGVLTANAIF KGSGHLNPAI SLFYAINGSI KSPTALIWPG FVIGILAQFL GAMIAQTTLN FLFWKQLSST DPQTVLAMHC TSPSVFNITR NFLTEFIATL ILIGGVVAAS HFLHNNPNSV PPGFMGLWLV AGIIIAFGGA TGSAINPARD LGTRIVFQLT PIKNKDANWK YSWIPVIAPL SAGLVLSIII GFSPAPVL // ID GLYA_MYCGE Reviewed; 406 AA. AC P47634; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 110. 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}; OrderedLocusNames=MG394; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-228. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71622.1; -; Genomic_DNA. DR EMBL; U02131; AAD12409.1; -; Genomic_DNA. DR PIR; F64243; F64243. DR RefSeq; WP_009885629.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47634; -. DR SMR; P47634; 5-402. DR STRING; 243273.MgenG_010200000540; -. DR EnsemblBacteria; AAC71622; AAC71622; MG_394. DR KEGG; mge:MG_394; -. DR PATRIC; 20010374; VBIMycGen98045_0460. DR eggNOG; ENOG4105C65; Bacteria. DR eggNOG; COG0112; LUCA. DR KO; K00600; -. DR OMA; KTYAQNV; -. DR OrthoDB; EOG6Z0QB2; -. DR BioCyc; MGEN243273:GH2R-451-MONOMER; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000000807; 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 1 406 Serine hydroxymethyltransferase. FT /FTId=PRO_0000113609. FT REGION 115 117 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT REGION 340 342 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 25 25 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 45 45 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 47 47 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 54 54 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 55 55 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 89 89 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 111 111 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00051}. FT BINDING 166 166 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 194 194 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 219 219 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 226 226 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 252 252 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 348 348 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT MOD_RES 220 220 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00051}. SQ SEQUENCE 406 AA; 44750 MW; C1D9280FE12071E2 CRC64; MFSKVRLLLN KELQRQRENI CLIASENYVS QDILAVTGSV LTNKYAEGYP SKRFYQGCEV VDESENLAIE SCKTLFGAQW ANVQPHSGSS ANYAVYLALL KPGDTILGLD LNCGGHLTHG SPVNFSGKQY QAVTYSLDFE TETLDYDAIL QIALEHKPKL IICGFSNYSR TVDFKKFSAI AKQVNAYLLA DIAHIAGFIA AGLHQNPLPF VDVVTSTTHK TLRGPRGGII MSNNQAIIKK LDSGVFPGCQ GGPLQHVIAA KYVCFKEALN PKFKQYMQQV KDNALAMANW FLKQGYRVVS KGTETHLFSL VVGNGKDVAL WLQKANIVLN MNTIPFETKS AFSPSGIRLG TPAMTTRGFK TNDFIFVASL IDKVIKSNGN QKVISQTKTA VLNLLKRFPL YKGLAY // ID GPMI_MYCGE Reviewed; 507 AA. AC P47669; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01038}; DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01038}; DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01038}; DE Short=iPGM {ECO:0000255|HAMAP-Rule:MF_01038}; DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01038}; GN Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; Synonyms=pgm; GN OrderedLocusNames=MG430; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and CC 3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01038}. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate. CC {ECO:0000255|HAMAP-Rule:MF_01038}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01038}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01038}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP- CC Rule:MF_01038}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01038}. CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase CC family. {ECO:0000255|HAMAP-Rule:MF_01038}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC72451.1; -; Genomic_DNA. DR PIR; E64247; E64247. DR ProteinModelPortal; P47669; -. DR STRING; 243273.MgenG_010200000310; -. DR PRIDE; P47669; -. DR EnsemblBacteria; AAC72451; AAC72451; MG_430. DR KEGG; mge:MG_430; -. DR PATRIC; 20010446; VBIMycGen98045_0496. DR eggNOG; ENOG4105CJI; Bacteria. DR eggNOG; COG0696; LUCA. DR KO; K15633; -. DR OrthoDB; EOG6HJ22X; -. DR BioCyc; MGEN243273:GH2R-484-MONOMER; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1450.10; -; 1. DR Gene3D; 3.40.720.10; -; 2. DR HAMAP; MF_01038; GpmI; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR011258; BPG-indep_PGM_N. DR InterPro; IPR006124; Metalloenzyme. DR InterPro; IPR005995; Pgm_bpd_ind. DR Pfam; PF06415; iPGM_N; 1. DR Pfam; PF01676; Metalloenzyme; 1. DR PIRSF; PIRSF001492; IPGAM; 1. DR SUPFAM; SSF53649; SSF53649; 2. DR SUPFAM; SSF64158; SSF64158; 1. DR TIGRFAMs; TIGR01307; pgm_bpd_ind; 1. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Isomerase; Manganese; Metal-binding; KW Reference proteome. FT CHAIN 1 507 2,3-bisphosphoglycerate-independent FT phosphoglycerate mutase. FT /FTId=PRO_0000212167. FT REGION 150 151 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT REGION 257 260 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT ACT_SITE 61 61 Phosphoserine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01038}. FT METAL 11 11 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 61 61 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 397 397 Manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 401 401 Manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 438 438 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 439 439 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT METAL 456 456 Manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT BINDING 122 122 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT BINDING 182 182 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT BINDING 188 188 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01038}. FT BINDING 332 332 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01038}. SQ SEQUENCE 507 AA; 56867 MW; 9BD9F5007C9CBEB5 CRC64; MHKKVLLAIL DGYGISNAIY GNAVQNANTP MLDELINSYP CVLLDASGEA VGLPMGQIGN SEVGHLNIGA GRVVYTGLSL INQHIKDRSF FANKAFLKTI EHVEKNHSKI HLIGLFSNGG VHSHNEHLLA LIELFSKHAK VVLHLFGDGR DVAPCSLKQD LEKLMIFLKN YPNVVIGTIG GRYYGMDRDQ RWDREMIAYK ALLGVSKNKF NDPIGYIETQ YQNQITDEFI YPAINANLNS DQFALNNNDG VISFNFRPDR ARQMSHLIFN SNYYNYQPEL KRKENLFFVT MMNYEGIVPS EFAFPPQTIK NSLGEVIANN NLKQLRIAET EKYAHVTFFF DGGFEVNLSN ETKTLIPSLK VATYDLAPEM SCKAITDALL EKLNNFDFTV LNFANPDMVG HTGNYQACIK ALEALDVQIK RIVDFCKANQ ITMFLTADHG NAEVMIDNNN NPVTKHTINP VPFVCTDKNV NFNQTGILAN IAPTILEYLN LSKPKEMTAK SLLKNNN // ID GREA_MYCGE Reviewed; 161 AA. AC P47524; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 100. 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}; OrderedLocusNames=MG282; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71504.1; -; Genomic_DNA. DR PIR; B64231; B64231. DR RefSeq; WP_009885993.1; NZ_AAGX01000018.1. DR ProteinModelPortal; P47524; -. DR STRING; 243273.MgenG_010200003275; -. DR EnsemblBacteria; AAC71504; AAC71504; MG_282. DR KEGG; mge:MG_282; -. DR PATRIC; 20010074; VBIMycGen98045_0324. DR eggNOG; ENOG4107YHV; Bacteria. DR eggNOG; COG0782; LUCA. DR KO; K03624; -. DR OMA; HNEGRIA; -. DR OrthoDB; EOG686NQ9; -. DR BioCyc; MGEN243273:GH2R-316-MONOMER; -. DR Proteomes; UP000000807; 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 1 161 Transcription elongation factor GreA. FT /FTId=PRO_0000176939. FT COILED 8 28 {ECO:0000255|HAMAP-Rule:MF_00105}. SQ SEQUENCE 161 AA; 18163 MW; 67E2850CB59BCC5B CRC64; MELNKNYLTQ EGFKQLEKEL ENLIQVKRPE IIRLLQEARD QGDLSENADY DAAKAQQGEI ETRIAEIQDI LANAKLISDH QAKTKVTKVS LGSTVEIYDY SSKSNEKYTI VGTLEANPEE HKISNESPLA LAIYGRLIGD ECDVVGIEVP YRVKILKISN R // ID GYRA_MYCGE Reviewed; 836 AA. AC P47250; Q49325; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 102. 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}; OrderedLocusNames=MG004; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8083173; RA Bailey C.C., Bott K.F.; RT "An unusual gene containing a dnaJ N-terminal box flanks the putative RT origin of replication of Mycoplasma genitalium."; RL J. Bacteriol. 176:5814-5819(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77 AND 205-302. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 509-639. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). 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; U09251; AAA57072.1; -; Genomic_DNA. DR EMBL; L43967; AAC71220.1; -; Genomic_DNA. DR EMBL; U02211; AAD12504.1; -; Genomic_DNA. DR EMBL; U01696; AAB01009.1; -; Genomic_DNA. DR EMBL; X61533; CAA43745.1; -; Genomic_DNA. DR PIR; D64200; D64200. DR RefSeq; WP_009885559.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47250; -. DR STRING; 243273.MgenG_010200000025; -. DR PRIDE; P47250; -. DR EnsemblBacteria; AAC71220; AAC71220; MG_004. DR KEGG; mge:MG_004; -. DR PATRIC; 20009384; VBIMycGen98045_0004. DR eggNOG; ENOG4105C24; Bacteria. DR eggNOG; COG0188; LUCA. DR KO; K02469; -. DR OMA; ESYLAYS; -. DR OrthoDB; EOG661H5V; -. DR BioCyc; MGEN243273:GH2R-4-MONOMER; -. DR Proteomes; UP000000807; 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:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. 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 1 836 DNA gyrase subunit A. FT /FTId=PRO_0000145240. FT MOTIF 537 543 GyrA-box. {ECO:0000255|HAMAP- FT Rule:MF_01897}. FT ACT_SITE 134 134 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01897}. FT CONFLICT 68 76 GMHHDRPFK -> WSCTMIVLL (in Ref. 3; FT AAD12504). {ECO:0000305}. FT CONFLICT 648 648 R -> L (in Ref. 1; AAA57072). FT {ECO:0000305}. SQ SEQUENCE 836 AA; 93682 MW; 364A78ED5B060BCE CRC64; MAKQQDQVDK IRENLDNSTV KSISLANELE RSFMEYAMSV IVARALPDAR DGLKPVHRRV LYGAYIGGMH HDRPFKKSAR IVGDVMSKFH PHGDMAIYDT MSRMAQDFSL RYLLIDGHGN FGSIDGDRPA AQRYTEARLS KLAAELLKDI DKDTVDFIAN YDGEEKEPTV LPAAFPNLLA NGSSGIAVGM STSIPSHNLS ELIAGLIMLI DNPQCTFQEL LTVIKGPDFP TGANIIYTKG IESYFETGKG NVVIRSKVEI EQLQTRSALV VTEIPYMVNK TTLIEKIVEL VKAEEISGIA DIRDESSREG IRLVIEVKRD TVPEVLLNQL FKSTRLQVRF PVNMLALVKG APVLLNMKQA LEVYLDHQID VLVRKTKFVL NKQQERYHIL SGLLIAALNI DEVVAIIKKS ANNQEAINTL NTKFKLDEIQ AKAVLDMRLR SLSVLEVNKL QTEQKELKDS IEFCKKVLAD QKLQLKIIKE ELQKINDQFG DERRSEILYD ISEEIDDESL IKVENVVITM STNGYLKRIG VDAYNLQHRG GVGVKGLTTY VDDSISQLLV CSTHSDLLFF TDKGKVYRIR AHQIPYGFRT NKGIPAVNLI KIEKDERICS LLSVNNYDDG YFFFCTKNGI VKRTSLNEFI NILSNGKRAI SFDDNDTLYS VIKTHGNDEI FIGSTNGFVV RFHENQLRVL SRTARGVFGI SLNKGEFVNG LSTSSNGSLL LSVGQNGIGK LTSIDKYRLT KRNAKGVKTL RVTDRTGPVV TTTTVFGNED LLMISSAGKI VRTSLQELSE QGKNTSGVKL IRLKDNERLE RVTIFKEELE DKEMQLEDVG SKQITQ // ID GRPE_MYCGE Reviewed; 217 AA. AC P47443; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 91. 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}; OrderedLocusNames=MG201; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71419.1; -; Genomic_DNA. DR PIR; B64222; B64222. DR RefSeq; WP_009885741.1; NZ_AAGX01000004.1. DR ProteinModelPortal; P47443; -. DR STRING; 243273.MgenG_010200001342; -. DR EnsemblBacteria; AAC71419; AAC71419; MG_201. DR KEGG; mge:MG_201; -. DR PATRIC; 20009854; VBIMycGen98045_0233. DR eggNOG; ENOG4107ZRJ; Bacteria. DR eggNOG; COG0576; LUCA. DR KO; K03687; -. DR OMA; MERMQIM; -. DR OrthoDB; EOG64BQ6C; -. DR BioCyc; MGEN243273:GH2R-209-MONOMER; -. DR Proteomes; UP000000807; 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 1 217 Protein GrpE. FT /FTId=PRO_0000113816. SQ SEQUENCE 217 AA; 25014 MW; 9643920BB7084003 CRC64; MCEKSQTIKE LLNAIRTLVV KNNKAKVSMI EKELLAFVSE LDKKFKQQLN NFNELQQKIP LLQKANEEFA LKFERMQREA QNQIQAKLDE LNLKNKKELE QAKKYAIAKT LDQPLNIIDQ FEIALSYAQK DPQVKNYTTG FTMVLDAFSR WLEANGVTKI KIEPGMEFDE KIMSALELVD SNLAKNKVVR VSKSGYKLYD KVIRFASVFV SKGNKKS // ID GYRB_MYCGE Reviewed; 650 AA. AC P47249; Q49307; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 105. 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}; OrderedLocusNames=MG003; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8083173; RA Bailey C.C., Bott K.F.; RT "An unusual gene containing a dnaJ N-terminal box flanks the putative RT origin of replication of Mycoplasma genitalium."; RL J. Bacteriol. 176:5814-5819(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-304; 404-507 AND 605-650. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; U09251; AAA57071.1; -; Genomic_DNA. DR EMBL; L43967; AAC71219.1; -; Genomic_DNA. DR EMBL; U02187; AAD12471.1; -; Genomic_DNA. DR EMBL; U02199; AAD12487.1; -; Genomic_DNA. DR EMBL; U02211; AAD12503.1; -; Genomic_DNA. DR PIR; C64200; C64200. DR RefSeq; WP_009885560.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47249; -. DR STRING; 243273.MgenG_010200000030; -. DR EnsemblBacteria; AAC71219; AAC71219; MG_003. DR KEGG; mge:MG_003; -. DR PATRIC; 20009382; VBIMycGen98045_0003. DR eggNOG; ENOG4105C7D; Bacteria. DR eggNOG; COG0187; LUCA. DR KO; K02470; -. DR OMA; IKNMITA; -. DR OrthoDB; EOG6P334W; -. DR BioCyc; MGEN243273:GH2R-3-MONOMER; -. DR Proteomes; UP000000807; 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:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) 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 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 1 650 DNA gyrase subunit B. FT /FTId=PRO_0000145319. FT DOMAIN 435 549 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT METAL 441 441 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01898}. FT METAL 514 514 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01898}. FT METAL 514 514 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT METAL 516 516 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT SITE 466 466 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT SITE 469 469 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_01898}. SQ SEQUENCE 650 AA; 73605 MW; 750BA6035A5CB55E CRC64; MEENNKANIY DSSSIKVLEG LEAVRKRPGM YIGSTGEEGL HHMIWEIVDN SIDEAMGGFA SFVKLTLEDN FVTRVEDDGR GIPVDIHPKT NRSTVETVFT VLHAGGKFDN DSYKVSGGLH GVGASVVNAL SSSFKVWVFR QNKKYFLSFS DGGKVIGDLV QEGNSEKEHG TIVEFVPDFS VMEKSDYKQT VIVSRLQQLA FLNKGIRIDF VDNRKQNPQS FSWKYDGGLV EYIHHLNNEK EPLFNEVIAD EKTETVKAVN RDENYTVKVE VAFQYNKTYN QSIFSFCNNI NTTEGGTHVE GFRNALVKII NRFAVENKFL KDSDEKINRD DVCEGLTAII SIKHPNPQYE GQTKKKLGNT EVRPLVNSVV SEIFERFMLE NPQEANAIIR KTLLAQEARR RSQEARELTR RKSPFDSGSL PGKLADCTTR DPSISELYIV EGDSAGGTAK TGRDRYFQAI LPLRGKILNV EKSNFEQIFN NAEISALVMA IGCGIKPDFE LEKLRYSKIV IMTDADVDGA HIRTLLLTFF FRFMYPLVEQ GNIFIAQPPL YKVSYSHKDL YMHTDVQLEQ WKSQNPNVKF GLQRYKGLGE MDALQLWETT MDPKVRTLLK VTVEDASIAD KAFSLLMGDE VPPRREFIEK NARSVKNIDI // ID HMW2_MYCGE Reviewed; 1805 AA. AC P47460; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=Cytadherence high molecular weight protein 2; DE AltName: Full=Cytadherence accessory protein 2; GN Name=hmw2; OrderedLocusNames=MG218; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 557-659. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Component of the cytoskeleton-like structure which CC stabilizes the shape of the wall-less Mycoplasma. This CC cytoskeleton-like network of accessory proteins containing HMW CC proteins 1 to 5 allows the proper anchoring of cytadhesin proteins CC in the mycoplasmal membrane at the attachment organelle (By CC similarity). {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71437.1; -; Genomic_DNA. DR EMBL; U02165; AAD12447.1; -; Genomic_DNA. DR PIR; A64224; A64224. DR RefSeq; WP_010869377.1; NC_000908.2. DR ProteinModelPortal; P47460; -. DR EnsemblBacteria; AAC71437; AAC71437; MG_218. DR KEGG; mge:MG_218; -. DR PATRIC; 20009912; VBIMycGen98045_0253. DR OMA; QAFNQIN; -. DR OrthoDB; EOG6N3CNZ; -. DR BioCyc; MGEN243273:GH2R-238-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0020035; P:cytoadherence to microvasculature, mediated by symbiont protein; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR016430; Cytadherence_Hmw2. DR PIRSF; PIRSF004800; Hmw2; 1. PE 3: Inferred from homology; KW Coiled coil; Complete proteome; Cytadherence; Reference proteome; KW Virulence. FT CHAIN 1 1805 Cytadherence high molecular weight FT protein 2. FT /FTId=PRO_0000084013. FT COILED 28 838 {ECO:0000255}. FT COILED 914 1591 {ECO:0000255}. FT COILED 1632 1723 {ECO:0000255}. FT COILED 1777 1804 {ECO:0000255}. SQ SEQUENCE 1805 AA; 216253 MW; 11D093AF173284FD CRC64; MKPFDKKPSL QPIYDIGFDD GYLQSEYEKN RSKTDVDKIE NQLLKEIKSL EDELKNLKGL KNQAEDNPEL DKKINHLEVD LNRLVNEYKN FQFQKNHMVD KVSELDNLTR FYKNELTRLQ QENADFLNSK YANLANFQAN YHNKLNDFHR LIENQNQTIN RLNQKINGNQ NLIDNNVALL QNPNITVEKK NYLLNVIDQL YNELDQLENQ KRLLSIEYEN TYRELVSADN ELQNVYENID QNQIQFKHQY QTYRDELSQL ERKIQLTKQE LVDKESALRV KIDDADFYIN ARLAELDDVA KQLSFQDGIT KQNAQHVEDK LVALNKEKDR LNTQKEAFFN LRQSALIDIN KLQQENELFA KHLEHQQNEF EQKQSDSLLK LETEYKALQH KINEFKNESA TKSEELLNQE RELFEKRREI DTLLTQASLE YEHQRESSQL LKDKQNEVKQ HFQNLEYAKK ELDKERNLLD QQKKVDSEAI FQLKEKVAQE RKELEELYLV KKQKQDQKEN ELLFFEKQLK QHQADFENEL EAKQQELFEA KHALERSFIK LEDKEKDLNT KAQQIANEFS QLKTDKSKSA DFELMLQNEY ENLQQEKQKL FQERTYFERN AAVLSNRLQQ KREELLQQKE TLDQLTKSFE QERLINQREH KELVASVEKQ KEILGKKLQD FSQTSLNASK NLAEREMAIK FKEKEIEATE KQLLNDVNNA EVIQADLAQL NQSLNQERSE LQNAKQRIAD FHNDSLKKLN EYELSLQKRL QELQTLEANQ KQHSYQNQAY FEGELDKLNR EKQAFLNLRK KQTMEVDAIK QRLSDKHQAL NMQQAELDRK THELNNAFLN HDADQKSLQD QLATVKETQK LIDLERSALL EKQREFAENV AGFKRHWSNK TSQLQKIYEL TKKQESEQTQ KETELKIAFS DLQKDYQVFE LQKDQEFRQI EAKQRELDKL AEKNNQVKLE LDNRFQALQN QKQDTVQAQL ELEREQHQLN LEQTAFNQAN ESLLKQREQL TKKIQAFHYE LKKRNQFLAL KGKRLFAKEQ DQQRKDQEIN WRFKQFEKEY TDFDEAKKRE LEELEKIRRS LSQSNVELER KREKLATDFT NLNKVQHNTQ INRDQLNSQI RQFLLERKNF QRFSNEANAK KAFLIKRLRS FASNLKLQKE ALAIQKLEFD KRDEQQKKEL QQATLQLEQF KFEKQNFDIE KQRQLVAIKT QCEKLSDEKK ALNQKLVELK NLSQTYLANK NKAEYSQQQL QQKYTNLLDL KENLERTKDQ LDKKHRSIFA RLTKFANDLR FEKKQLLKAQ RIVDDKNRLL KENERNLHFL SNETERKRAV LEDQISYFEK QRKQATDAIL ASHKEVKKKE GELQKLLVEL ETRKTKLNND FAKFSRQREE FENQRLKLLE LQKTLQTQTN SNNFKTKAIQ EIENSYKRGM EELNFQKKEF DKNKSRLYEY FRKMRDEIER KESQVKLVLK ETQRKANLLE AQANKLNIEK NTIDFKEKEL KAFKDKVDQD IDSTNKQRKE LNELLNENKL LQQSLIERER AINSKDSLLN KKIETIKRQL HDKEMRVLRL VDRMKLAEQK YQTEINRLRT QTFDSEKQDI KNFFPPLFKI NGNDMAFPYL YPWLYPQQKQ DDNTLQIRQL FEQQLQFMQQ RYENELNELR RQRNLLEKKL DQIQLESQLN NKQSEFSKVE SMMEKLLEKT ESRLNDFDQK INYLTKKVNQ HNTYQPSSYQ PTPSYQDSDK QQLLFRIQEL EKQNLFQQQF QPAPAVVQQP TSFAAPNITK QQQIAQLNAE INNIKRLIAQ KAASK // ID HPRK_MYCGE Reviewed; 311 AA. AC P47331; Q49232; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=HPr kinase/phosphorylase; DE Short=HPrK/P; DE EC=2.7.11.-; DE EC=2.7.4.-; DE AltName: Full=HPr(Ser) kinase/phosphorylase; GN Name=hprK; OrderedLocusNames=MG085; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Catalyzes the ATP- as well as the pyrophosphate- CC dependent phosphorylation of a specific serine residue in HPr, a CC phosphocarrier protein of the phosphoenolpyruvate-dependent sugar CC phosphotransferase system (PTS). HprK/P also catalyzes the CC pyrophosphate-producing, inorganic phosphate-dependent CC dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P- CC Ser-HPr) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + HPr = ADP + P-Ser-HPr. CC -!- CATALYTIC ACTIVITY: P-Ser-HPr + phosphate = HPr + diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Homohexamer. {ECO:0000250}. CC -!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi. CC {ECO:0000250}. CC -!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried CC out by the same active site and suggest a common mechanism for CC both reactions. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HPrK/P 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; L43967; AAC71303.1; -; Genomic_DNA. DR EMBL; U01783; AAD10604.1; -; Genomic_DNA. DR PIR; D64209; D64209. DR RefSeq; WP_010869325.1; NC_000908.2. DR ProteinModelPortal; P47331; -. DR SMR; P47331; 1-311. DR EnsemblBacteria; AAC71303; AAC71303; MG_085. DR KEGG; mge:MG_085; -. DR PATRIC; 20009572; VBIMycGen98045_0095. DR KO; K06023; -. DR OMA; AVRRKMR; -. DR OrthoDB; EOG6F55HT; -. DR BioCyc; MGEN243273:GH2R-88-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1390.20; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01249; HPr_kinase; 1. DR InterPro; IPR003755; HPr(Ser)_kin/Pase. DR InterPro; IPR011104; Hpr_kin/Pase_C. DR InterPro; IPR011126; Hpr_kin/Pase_Hpr_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR028979; Ser_kin/Pase_Hpr_N-like. DR Pfam; PF07475; Hpr_kinase_C; 1. DR Pfam; PF02603; Hpr_kinase_N; 1. DR SUPFAM; SSF75138; SSF75138; 1. DR TIGRFAMs; TIGR00679; hpr-ser; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; KW Magnesium; Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 311 HPr kinase/phosphorylase. FT /FTId=PRO_0000058970. FT NP_BIND 154 161 ATP. {ECO:0000250}. FT REGION 201 210 Important for the catalytic mechanism of FT both phosphorylation and FT dephosphorylation. {ECO:0000250}. FT REGION 266 271 Important for the catalytic mechanism of FT dephosphorylation. {ECO:0000250}. FT ACT_SITE 139 139 {ECO:0000250}. FT ACT_SITE 160 160 {ECO:0000250}. FT ACT_SITE 178 178 Proton acceptor; for phosphorylation FT activity. Proton donor; for FT dephosphorylation activity. FT {ECO:0000250}. FT ACT_SITE 245 245 {ECO:0000250}. FT METAL 161 161 Magnesium. {ECO:0000255}. FT METAL 202 202 Magnesium. {ECO:0000255}. FT CONFLICT 58 62 KREFI -> NVIYF (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 311 AA; 34686 MW; F53F5FD9BA04E4C9 CRC64; MKHLTVKALV LQFNDCIQLI DGKNNIDNVI TIPGLKRSVF ELLGLFCKPI GSVAILGKRE FIFLNQKPVE QQKKIIANLL KLKPPAVILT KSFLDCGVLL AVNQTYQVPI LKTNLFSTEL SFTVETYINE QFATVQKLHG VLLEIFGVGV FLEGKSGIGK SESALDLINK NHLLIGDDAI EIYRLGNRLF GRAQALAKGF MEIRGLGIIN IERAYGLQIT KEQTEIQLAI SLLSLEEKNN ASFERLGSDL KLKNLLGVKI SYYQIPISSG RKTSEIIESA VIDFKLKKSG YNSANEFILK QRAMLEEQTD E // ID HPRR_MYCGE Reviewed; 141 AA. AC P47666; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 74. DE RecName: Full=Hydroperoxide reductase; DE EC=1.11.1.-; GN OrderedLocusNames=MG427; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP FUNCTION AS A PEROXIDASE, SUBCELLULAR LOCATION, INDUCTION, AND RP DISRUPTION PHENOTYPE. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=24363346; DOI=10.1128/JB.00954-13; RA Zhang W., Baseman J.B.; RT "Functional characterization of osmotically inducible protein C RT (MG_427) from Mycoplasma genitalium."; RL J. Bacteriol. 196:1012-1019(2014). CC -!- FUNCTION: Reduces organic and inorganic peroxide substrates. CC Protects the cell against oxidative stress. CC {ECO:0000269|PubMed:24363346}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24363346}. CC Note=A small fraction is associated with the cell membrane. CC -!- INDUCTION: Down-regulated by osmotic shock and ethanol. Not CC induced by oxidative stress. {ECO:0000269|PubMed:24363346}. CC -!- DISRUPTION PHENOTYPE: Mutant is highly sensitive to killing by CC tert-butyl hydroperoxide (t-BHP) and H(2)O(2). CC {ECO:0000269|PubMed:24363346}. CC -!- SIMILARITY: Belongs to the OsmC/Ohr 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; L43967; AAC72448.1; -; Genomic_DNA. DR PIR; B64247; B64247. DR RefSeq; WP_009885605.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47666; -. DR SMR; P47666; 1-141. DR STRING; 243273.MgenG_010200000330; -. DR EnsemblBacteria; AAC72448; AAC72448; MG_427. DR KEGG; mge:MG_427; -. DR PATRIC; 20010440; VBIMycGen98045_0493. DR eggNOG; ENOG410815Q; Bacteria. DR eggNOG; COG1765; LUCA. DR OMA; ELSVISY; -. DR OrthoDB; EOG6Z9B4B; -. DR BioCyc; MGEN243273:GH2R-481-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. 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 Complete proteome; Cytoplasm; Oxidoreductase; Peroxidase; KW Reference proteome. FT CHAIN 1 141 Hydroperoxide reductase. FT /FTId=PRO_0000210606. SQ SEQUENCE 141 AA; 15603 MW; CF64701E8AEFE393 CRC64; MDKKYDITAV LNDDSSINAV SDNFQITLDA RPKEKSKGIN PLSAFLAGLA ACELATANAM AAAKMITLNK ALINIKGYRL TNPSDGYFGL RELNIHWEIH SPNEEEEIKE FIDFVSKRCP AHNTLHGTSN FKINISVTLV H // ID HMW1_MYCGE Reviewed; 1139 AA. AC Q49413; Q49365; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Cytadherence high molecular weight protein 1; DE AltName: Full=Cytadherence accessory protein 1; GN Name=hmw1; OrderedLocusNames=MG312; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 721-847. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Component of the cytoskeleton-like structure which CC stabilizes the shape of the wall-less Mycoplasma. This CC cytoskeleton-like network of accessory proteins containing HMW CC proteins 1 to 5 allows the proper anchoring of cytadhesin proteins CC in the mycoplasmal membrane at the attachment organelle (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell projection, attachment organelle CC membrane {ECO:0000250}. Note=Localizes specifically to the CC attachment membrane. {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71534.1; -; Genomic_DNA. DR EMBL; U02261; AAD12527.1; -; Genomic_DNA. DR PIR; E64234; E64234. DR RefSeq; WP_010869424.1; NC_000908.2. DR EnsemblBacteria; AAC71534; AAC71534; MG_312. DR KEGG; mge:MG_312; -. DR PATRIC; 20010154; VBIMycGen98045_0363. DR OrthoDB; EOG6DVJQC; -. DR BioCyc; MGEN243273:GH2R-348-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0033111; C:attachment organelle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0020035; P:cytoadherence to microvasculature, mediated by symbiont protein; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR022466; AGR_box. DR InterPro; IPR021199; Cytadherence_HMW-1_N. DR Pfam; PF16713; EAGR_box; 1. DR TIGRFAMs; TIGR03834; EAGR_box; 1. DR TIGRFAMs; TIGR03836; termin_org_HMW1; 1. PE 3: Inferred from homology; KW Cell membrane; Cell projection; Coiled coil; Complete proteome; KW Cytadherence; Membrane; Reference proteome; Virulence. FT CHAIN 1 1139 Cytadherence high molecular weight FT protein 1. FT /FTId=PRO_0000084011. FT COILED 902 935 {ECO:0000255}. FT COILED 974 1025 {ECO:0000255}. SQ SEQUENCE 1139 AA; 130531 MW; 0011D3288C3DD856 CRC64; MAKNKQSVFE EKNYTQTEPE NIFGDLYDGK STVEEDPNIK VAYDADGNGY YIAFNKETGV YYDPYGDTEY DISQLFDENG NPFVFDEKQE ENDYLKYVGN PDYGSYDENG EWVWSGYFEN DQWISTKESQ PTDENYGFDS DLPPEVKQPE SVEDNYGFDN DLPPEVKQPE SVEDNYGFDN DLPPEVKQPE SVVDQPSSDD YFAKQPTDEN YGFDNDLPPE VKQPESVVDQ PSSDDHFAKQ PESTTDSYSF DSDLPQPTLD QPSLDDHVQY NFDHHEELKP VAEEQNNYQV GFDQVQANLD NNEEIQPTAE KKVTTDFESK QAQVVDSYQL PIDTDQQDQT TFSSSFETQP TVEQFDQVNS EVNDQFKPEI TKEPVLESSF NKQDVVETSD LNSESNLYSE NNKDATNNDS LNSEFIQLNS NSETASDDVH YESKSEPIHD YKFGSDLSQS NSNNSLESEP VKFNSETAPD AHFESQSEPV DQVQYDIYQN EELKPTLDQP SSDDYFAKQP TDENYGFDND LPPEVKQPES VVDQPSSDDH FAKQPESTTD SYSFDSDLPQ PTLDQPSLDD HVQYNFDHHE ELKPVAEEQN NYQVGFDQVQ ANLDNNEEIQ PTAEKEVTTD FESKQAQVVD SYQLPIDTDQ QDQTTFSSSF ETQPTVEQFD QVNSEVNDQF KPEITKEPVL ESSFNKQDVV ETSNYTNNLQ KFDIQSDNKI TITTKKSSPQ IPTTLPISFV SNRIEYKPVE TLALDNKESQ QEQITINSIT EDSKTLAKTL SVQLQQINSL NNQSIVTSES VRLDKKDDQL TINTVNSEDQ QPKIEVFVKA KEPVEEHSIT QNKQSVEDKS ELDNFNKKSD LYKIISELKR GELNPTINFD AIFQMNDYQM SVKQSFIHLN DFVTNYKNQI SERYLIIKKE LQSELSRLID QNENLNVQFN NAKNLTTLQK EEMIRSLASD FAIAYKPSNS YEQLQKSGEI MRHVQRAITE NEKKIESIQG SLKQLKTVYN SCCETIMNNI NKLDNTLRFA KKEKDPLLLS NFDSVTDNGL VEPNQLMDDL IDFSNTFDNI SNEQLDDFIY ENMDRNIDFE FEGFNNDFVD IDAKVMDSMS AFSVNDLDIE TLVPDRTSNF SSLLDEDLFE SSGDFSLDY // ID HMW3_MYCGE Reviewed; 599 AA. AC Q57081; Q49191; Q49337; Q49370; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=Cytadherence high molecular weight protein 3; DE AltName: Full=Accessory adhesin protein 3; DE AltName: Full=Cytadherence accessory protein 3; DE AltName: Full=P69; GN Name=hmw3; OrderedLocusNames=MG317; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7592348; RA Reddy S.P., Rasmussen W.G., Baseman J.B.; RT "Molecular cloning and characterization of an adherence-related operon RT of Mycoplasma genitalium."; RL J. Bacteriol. 177:5943-5951(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24; 57-169 AND 444-514. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Component of the cytoskeleton-like structure which CC stabilizes the shape of the wall-less mycoplasma. This CC cytoskeleton-like network of accessory proteins containing HMW CC proteins 1 to 5 allows the proper anchoring of cytadhesin proteins CC in the mycoplasmal membrane at the attachment organelle. Essential CC for successful surface parasitism (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell projection, attachment organelle CC membrane {ECO:0000250}. Note=Localizes specifically to the CC attachment membrane. {ECO:0000250}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC43190.1; 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; L43967; AAC71539.1; -; Genomic_DNA. DR EMBL; L43097; AAA99946.1; -; Genomic_DNA. DR EMBL; U01716; AAC43190.1; ALT_INIT; Unassigned_DNA. DR EMBL; U02224; AAA03378.1; -; Genomic_DNA. DR EMBL; U02267; AAD12533.1; -; Genomic_DNA. DR PIR; A64235; A64235. DR RefSeq; WP_010869426.1; NC_000908.2. DR EnsemblBacteria; AAC71539; AAC71539; MG_317. DR KEGG; mge:MG_317; -. DR PATRIC; 20010164; VBIMycGen98045_0368. DR OrthoDB; EOG6KT2N3; -. DR BioCyc; MGEN243273:GH2R-353-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0033111; C:attachment organelle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0020035; P:cytoadherence to microvasculature, mediated by symbiont protein; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW Cell membrane; Cell projection; Complete proteome; Cytadherence; KW Membrane; Reference proteome; Virulence. FT CHAIN 1 599 Cytadherence high molecular weight FT protein 3. FT /FTId=PRO_0000084015. SQ SEQUENCE 599 AA; 68721 MW; D786BE7BD491129A CRC64; MNDKQKAKIN KAYNKLLKKI NKRYPDVSVV YARDHKNKVH ALYQDPESGN IFSLEKRKQL ASNYPLFELT SDNPISFTNN IVSLNAYDDK NNLVTVQYDQ DNNTFYDQNG NVLDVSSYTD EKKVPLINYL SSTQTSQEQP TQQDYPSIDA GLPKIEVDDQ PKAAQHTTLE TESEPDVFEL NDSLNQPQQP TENLGDDQFV EKEVPPTQQL HQDLVHQQPV QVDSGSQNHS FNNSPSLKPP LVNKPAKLVQ PEVKHIPQVE VQPKPQIVEP KIEPKPEVKH VSHVEIQPKP EVKPVVDSVP EVKQPEVKHV PHVEVQPKPV VDLKPQRIEP RIESKPEVIK HIPQVEVQPK AQMVEPRIEP KPETKYIPQV ESTPQVEVHH WKPEVKTEYQ PQQPLPTSGL QIKVVPRSAA LLQSKLDTGF QPRQVERTTD SDITVSVSSH ASLLEKINAL NHQRIMSDIA LKSDNTIKSS NFSRFYPENE YVATKYSDPL YSDTNQSLTS DRFSLDFDYT PKSRVNNYTP LRSTNFQNNA ISNYRFSRTP SSYYPLTRRP WRLTNISSYR SSFHSPTRLS SFRRTSLPFS SSYDGLRRYP SRSYWSKDF // ID HPRT_MYCGE Reviewed; 175 AA. AC P47696; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase; DE Short=HGPRT; DE Short=HGPRTase; DE EC=2.4.2.8; GN Name=hpt; OrderedLocusNames=MG458; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-98. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: IMP + diphosphate = hypoxanthine + 5-phospho- CC alpha-D-ribose 1-diphosphate. CC -!- CATALYTIC ACTIVITY: GMP + diphosphate = guanine + 5-phospho-alpha- CC D-ribose 1-diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per subunit. The magnesium ions are CC essentially bound to the substrate and have few direct CC interactions with the protein. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; CC IMP from hypoxanthine: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase 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; L43967; AAC72478.1; -; Genomic_DNA. DR EMBL; U02193; AAD12479.1; -; Genomic_DNA. DR PIR; F64250; F64250. DR RefSeq; WP_009885573.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47696; -. DR STRING; 243273.MgenG_010200000135; -. DR EnsemblBacteria; AAC72478; AAC72478; MG_458. DR KEGG; mge:MG_458; -. DR PATRIC; 20010510; VBIMycGen98045_0528. DR eggNOG; ENOG4108UGV; Bacteria. DR eggNOG; COG0634; LUCA. DR KO; K00760; -. DR OMA; TMDWMAV; -. DR OrthoDB; EOG693GNP; -. DR BioCyc; MGEN243273:GH2R-511-MONOMER; -. DR UniPathway; UPA00591; UER00648. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase 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:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW. 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. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Magnesium; KW Metal-binding; Nucleotide-binding; Purine salvage; Reference proteome; KW Transferase. FT CHAIN 1 175 Hypoxanthine-guanine FT phosphoribosyltransferase. FT /FTId=PRO_0000139605. FT NP_BIND 96 105 IMP. {ECO:0000250}. FT NP_BIND 155 156 IMP. {ECO:0000250}. FT ACT_SITE 100 100 Proton acceptor. {ECO:0000250}. FT METAL 156 156 Magnesium. {ECO:0000250}. FT BINDING 128 128 IMP. {ECO:0000250}. SQ SEQUENCE 175 AA; 19759 MW; 9647332FFF3E18E0 CRC64; MGIKSIVINE QQIEEGCQKA VNWCNAKFNN KKVIVLGILK GCIPFLGKVI SKFSFDLQLD FMAVASYHGS HVQKQPPKIV LDMSHDPKDK DILLIEDIVD SGRSIKLVID LLKTRHAKSI TLISLIEKIK PKAFDINIDF SCFKVKDNFL VGFGLDYDGF YRNLPYVGVF EPDNP // ID HRCA_MYCGE Reviewed; 343 AA. AC P47447; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Heat-inducible transcription repressor HrcA {ECO:0000255|HAMAP-Rule:MF_00081}; GN Name=hrcA {ECO:0000255|HAMAP-Rule:MF_00081}; OrderedLocusNames=MG205; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71423.1; -; Genomic_DNA. DR PIR; F64222; F64222. DR RefSeq; WP_009885743.1; NZ_AAGX01000004.1. DR ProteinModelPortal; P47447; -. DR STRING; 243273.MgenG_010200001372; -. DR EnsemblBacteria; AAC71423; AAC71423; MG_205. DR KEGG; mge:MG_205; -. DR PATRIC; 20009864; VBIMycGen98045_0237. DR eggNOG; ENOG4105CI8; Bacteria. DR eggNOG; COG1420; LUCA. DR KO; K03705; -. DR OMA; IENESIW; -. DR OrthoDB; EOG632D4G; -. DR BioCyc; MGEN243273:GH2R-214-MONOMER; -. DR Proteomes; UP000000807; 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; 3.30.450.40; -; 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 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Repressor; Stress response; KW Transcription; Transcription regulation. FT CHAIN 1 343 Heat-inducible transcription repressor FT HrcA. FT /FTId=PRO_0000182503. SQ SEQUENCE 343 AA; 39513 MW; 18E66E169D8B346B CRC64; MKNLTPRQAQ ILKAIINEYI AYAIPVGSKL LTKKYFKNLS GGTLRNEMAA LEKKGFLKKN HISSGRVPSQ IGYQYYVKVL NVSNTTNDLK TRLRSVILQQ HKTIDEVIEL GVKFINEIIN LPVVLTNFSS DEVLKKIDLI ILDKSFALFL LVSASGKVFK KTISYANQRQ FEDIVICVRI FNDRIIDTRF SEINNQLEVL KEIIRTKVHE YQYVIDEILF KLFDLDQIEA NKKIYGIQYL AKQPEFANQE KLTKILNLLE DTSVWQQMAF INQTNQKTNI VFGDQLGFKE ISVASTLINT TSEAKHQLAI VGPTRMDYQK IKALLTTLKE EIEKYDKKIH NQT // ID IF1_MYCGE Reviewed; 70 AA. AC P47419; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075}; GN Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; OrderedLocusNames=MG173; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71391.1; -; Genomic_DNA. DR PIR; B64219; B64219. DR RefSeq; WP_009885858.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47419; -. DR STRING; 243273.MgenG_010200002269; -. DR EnsemblBacteria; AAC71391; AAC71391; MG_173. DR KEGG; mge:MG_173; -. DR PATRIC; 20009778; VBIMycGen98045_0195. DR eggNOG; ENOG4105K9U; Bacteria. DR eggNOG; COG0361; LUCA. DR KO; K02518; -. DR OMA; DERAPHT; -. DR OrthoDB; EOG6384SC; -. DR BioCyc; MGEN243273:GH2R-182-MONOMER; -. DR Proteomes; UP000000807; 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; IPR004368; TIF_IF1. DR Pfam; PF01176; eIF-1a; 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 70 Translation initiation factor IF-1. FT /FTId=PRO_0000095820. FT DOMAIN 1 70 S1-like. {ECO:0000255|HAMAP- FT Rule:MF_00075}. SQ SEQUENCE 70 AA; 8114 MW; 1EB8588B833C32F0 CRC64; MKNDKLFLTG KILEIIHGDK YRVMLENNVE VDAHLAGKMK MKRTKILPGD VVEVEFSPYD LKLGRITQRK // ID IF2_MYCGE Reviewed; 619 AA. AC P47388; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=Translation initiation factor IF-2; GN Name=infB; OrderedLocusNames=MG142; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-131. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71360.1; -; Genomic_DNA. DR EMBL; U01765; AAD10581.1; -; Genomic_DNA. DR PIR; G64215; G64215. DR RefSeq; WP_010869352.1; NC_000908.2. DR ProteinModelPortal; P47388; -. DR EnsemblBacteria; AAC71360; AAC71360; MG_142. DR KEGG; mge:MG_142; -. DR PATRIC; 20009714; VBIMycGen98045_0163. DR KO; K02519; -. DR OMA; LWYHSKV; -. DR OrthoDB; EOG67HJSV; -. DR BioCyc; MGEN243273:GH2R-150-MONOMER; -. DR Proteomes; UP000000807; 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; 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 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. DR PROSITE; PS01176; IF2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Initiation factor; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 619 Translation initiation factor IF-2. FT /FTId=PRO_0000137221. FT DOMAIN 120 289 tr-type G. FT NP_BIND 129 136 GTP. {ECO:0000250}. FT NP_BIND 176 180 GTP. {ECO:0000250}. FT NP_BIND 230 233 GTP. {ECO:0000250}. FT REGION 129 136 G1. {ECO:0000250}. FT REGION 154 158 G2. {ECO:0000250}. FT REGION 176 179 G3. {ECO:0000250}. FT REGION 230 233 G4. {ECO:0000250}. FT REGION 266 268 G5. {ECO:0000250}. SQ SEQUENCE 619 AA; 67888 MW; 3CD52DC8247808EE CRC64; MKKNRAFNQV KKTKFDGRIK TSAKHQLRNV KTGVKDGVFI YKGPLTVSEF ASKTNIAVAN IIKHFFLNGL ALTVNSVLTN EQLADACVNF GFDFKMETEV THENIVANIQ FEDSDDLLQP RPPIVTIMGH VDHGKTSLLD TIRKTNVTAK EFGGITQKIG AYQVKNHQNK TITFIDTPGH EAFTLMRARG AKVTDIVVLV VAADDGIKKQ TEEAISHAKS ANTPIIVFIN KMDKPTANPD LVIQQLNKFD LVPEAWGGKT IFVMGSALTG QGINELLDNI LLLGEVEGYQ ANYNAHSSGY AIEVQTSKGL GPIANVIVKR GTLKLGDIVV LGPAYGRVRT MHDENGNSLK QATPSKPVQI SGFDIMPVAG EKFIVFDDEK DAKLIANKFK EQQKQKANNL TVNQTLKEQI KNKEIKILNL IFKADSDGSL QAIKQAVENI NVAKISLSII HAAVGQISES DIMLAKASGA LLFSLNLGLS QTVKNIASLQ GVKLEVHYHI PKLAEEIENI LKGQLDPVYE EIEIGKAEVL QLWFHSKIGN IAGTIVKSGK IKRGNLCKLF RDKEIIFEGR IDSLKNEKTP VNLIETGKNC GIVINGCNDI KIGDIIVAYE KQIVKDGKL // ID IF3_MYCGE Reviewed; 184 AA. AC P47438; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 93. DE RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080}; GN Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; OrderedLocusNames=MG196; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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=AAC71414.1; 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; L43967; AAC71414.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; P47438; -. DR STRING; 243273.MgenG_010200001312; -. DR EnsemblBacteria; AAC71414; AAC71414; MG_196. DR KEGG; mge:MG_196; -. DR PATRIC; 20009844; VBIMycGen98045_0228. DR eggNOG; ENOG4108UUX; Bacteria. DR eggNOG; COG0290; LUCA. DR KO; K02520; -. DR OMA; SSHDIEW; -. DR OrthoDB; EOG63JRGJ; -. DR BioCyc; MGEN243273:GH2R-204-MONOMER; -. DR Proteomes; UP000000807; 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 1 184 Translation initiation factor IF-3. FT /FTId=PRO_0000177541. SQ SEQUENCE 184 AA; 21276 MW; 242517E716B3CC11 CRC64; MIQLAQNAKH PSKKEQKPLV NEQIAFNQFT LIDENSTNLG IVKMENALKL AQEKQLDLVL IAPNPTKPIV KLLDFGRYTY DLKRKKRQAK KNQTIIQTKE VVVKPTIAKH DLEFRAKQSK NWIEKGHHVK FIVRAFGRVS TRIELIEKVF DDFYQLVKDV VEIQKPLTAS SKTMYAALLV PLKR // ID IPYR_MYCGE Reviewed; 184 AA. AC P47593; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Inorganic pyrophosphatase; DE EC=3.6.1.1; DE AltName: Full=Pyrophosphate phospho-hydrolase; DE Short=PPase; GN Name=ppa; OrderedLocusNames=MG351; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 4 Mg(2+) ions per subunit. Other metal ions can support CC activity, but at a lower rate. Two Mg(2+) ions are required for CC the activation of the enzyme and are present before substrate CC binds, two additional Mg(2+) ions form complexes with substrate CC and product. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PPase 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; L43967; AAC71576.1; -; Genomic_DNA. DR PIR; H64238; H64238. DR RefSeq; WP_009885809.1; NZ_AAGX01000006.1. DR ProteinModelPortal; P47593; -. DR STRING; 243273.MgenG_010200001893; -. DR EnsemblBacteria; AAC71576; AAC71576; MG_351. DR KEGG; mge:MG_351; -. DR PATRIC; 20010278; VBIMycGen98045_0413. DR eggNOG; ENOG4105F0N; Bacteria. DR eggNOG; COG0221; LUCA. DR KO; K01507; -. DR OMA; EILGWQD; -. DR OrthoDB; EOG6NKR4X; -. DR BioCyc; MGEN243273:GH2R-405-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.90.80.10; -; 1. DR HAMAP; MF_00209; Inorganic_PPase; 1. DR InterPro; IPR008162; Pyrophosphatase. DR PANTHER; PTHR10286; PTHR10286; 1. DR Pfam; PF00719; Pyrophosphatase; 1. DR SUPFAM; SSF50324; SSF50324; 1. DR PROSITE; PS00387; PPASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 184 Inorganic pyrophosphatase. FT /FTId=PRO_0000137507. FT METAL 55 55 Magnesium 1. {ECO:0000250}. FT METAL 60 60 Magnesium 1. {ECO:0000250}. FT METAL 60 60 Magnesium 2. {ECO:0000250}. FT METAL 92 92 Magnesium 1. {ECO:0000250}. SQ SEQUENCE 184 AA; 21646 MW; 3A1F1006362FE3B9 CRC64; MDKFLIDVIV EIPKNSKIKY EYDRQTGQIR VDRILFGSES YPQNYGFIKN TLDWDGDELD CFIFADQPFL PATVVPTRIV GALEMIDDGE IDTKLLGVID CDPRYKEINQ ISDLPKHRIE EILIFLKTYK LLQKKTVIIK GLKDVCWAKK EYEICLQLMK DYGHLSKDQF IQKMQILHPE HYQK // ID KAD_MYCGE Reviewed; 214 AA. AC P47417; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 108. 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=MG171; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71389.1; -; Genomic_DNA. DR PIR; I64218; I64218. DR RefSeq; WP_009885856.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47417; -. DR STRING; 243273.MgenG_010200002259; -. DR EnsemblBacteria; AAC71389; AAC71389; MG_171. DR KEGG; mge:MG_171; -. DR PATRIC; 20009774; VBIMycGen98045_0193. DR eggNOG; ENOG4105CC8; Bacteria. DR eggNOG; COG0563; LUCA. DR KO; K00939; -. DR OMA; PHISTGA; -. DR OrthoDB; EOG679TH4; -. DR BioCyc; MGEN243273:GH2R-180-MONOMER; -. DR UniPathway; UPA00588; UER00649. DR Proteomes; UP000000807; 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; 2. DR SUPFAM; SSF57774; SSF57774; 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 1 214 Adenylate kinase. FT /FTId=PRO_0000158797. FT NP_BIND 15 20 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 62 64 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 90 93 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 137 138 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT REGION 35 64 NMPbind. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT REGION 127 164 LID. {ECO:0000255|HAMAP-Rule:MF_00235}. FT METAL 131 131 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT METAL 134 134 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT METAL 151 151 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT METAL 154 154 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT BINDING 36 36 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 41 41 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 97 97 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 128 128 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 161 161 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 172 172 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 200 200 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00235}. SQ SEQUENCE 214 AA; 24249 MW; C9F51652F24A600C CRC64; MVAQFNKFII LGPPGAGKGT VCKLLSKTTK LVHIASGDLF REAIKNQSVI GRKIAAIISQ GGYVDDATTN QLVYEYITTN PLPNGFILDG YPRTENQLDF LNIKLTIDMV FELVVSDLNK LITRIDNRVI CNNCNSVYNL LFQKPLVENS CDQCSAKLVK RSDDNKAVVK ARMELYQQTI QPIHTYFFNK QLLVQIDCFL PLEEQLKTIK QFIR // ID KGUA_MYCGE Reviewed; 240 AA. AC P47353; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 98. DE RecName: Full=Guanylate kinase; DE EC=2.7.4.8; DE AltName: Full=GMP kinase; GN Name=gmk; OrderedLocusNames=MG107; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC71325.1; 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; L43967; AAC71325.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; P47353; -. DR STRING; 243273.MgenG_010200000780; -. DR EnsemblBacteria; AAC71325; AAC71325; MG_107. DR KEGG; mge:MG_107; -. DR PATRIC; 20009618; VBIMycGen98045_0118. DR eggNOG; ENOG4108UHA; Bacteria. DR eggNOG; COG0194; LUCA. DR KO; K00942; -. DR OMA; MELQSIV; -. DR OrthoDB; EOG6CP410; -. DR BioCyc; MGEN243273:GH2R-111-MONOMER; -. DR Proteomes; UP000000807; 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; -; 2. DR HAMAP; MF_00328; Guanylate_kinase; 1. DR InterPro; IPR001270; ClpA/B. 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 PRINTS; PR00300; CLPPROTEASEA. 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 1 240 Guanylate kinase. FT /FTId=PRO_0000170562. FT DOMAIN 56 236 Guanylate kinase-like. FT NP_BIND 63 70 ATP. {ECO:0000250}. SQ SEQUENCE 240 AA; 27520 MW; 0664E11FE900935D CRC64; MIQVSICSSI GKLTASVGLL IKALSSKTSQ VLVGWKVIDK NSKVKIILTI EVNNQGRIFV ITGPSGVGKS TLVKALLDHF KEQLFYSISA TTRKKRISEK EGIDYFFKDK DEFENLIKQD AFIEWACYNN HYYGTLKSQA EQAIKSGINL MLEIEYQGAL QVKSKYPHNV VLIFIKPPSM QELLKRLKKR NDEDETTIKK RLEQAKIEFQ QIDNFKYVVT NKEFDKTLNE LKSILLSEFI // ID KTHY_MYCGE Reviewed; 210 AA. AC P47252; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=Thymidylate kinase; DE EC=2.7.4.9; DE AltName: Full=dTMP kinase; GN Name=tmk; OrderedLocusNames=MG006; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71222.1; -; Genomic_DNA. DR PIR; F64200; F64200. DR RefSeq; WP_009885557.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47252; -. DR STRING; 243273.MgenG_010200000015; -. DR EnsemblBacteria; AAC71222; AAC71222; MG_006. DR KEGG; mge:MG_006; -. DR PATRIC; 20009388; VBIMycGen98045_0006. DR eggNOG; ENOG4108ZMD; Bacteria. DR eggNOG; COG0125; LUCA. DR KO; K00943; -. DR OMA; NCFLING; -. DR OrthoDB; EOG64JFSH; -. DR BioCyc; MGEN243273:GH2R-6-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro. DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-HAMAP. 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 210 Thymidylate kinase. FT /FTId=PRO_0000155302. FT NP_BIND 11 18 ATP. {ECO:0000255}. SQ SEQUENCE 210 AA; 24248 MW; 10641CA5DCD202F6 CRC64; MNKGVFVVIE GVDGAGKTAL IEGFKKLYPT KFLNYQLTYT REPGGTLLAE KIRQLLLNET MEPLTEAYLF AAARTEHISK LIKPAIEKEQ LVISDRFVFS SFAYQGLSKK IGIDTVKQIN HHALRNMMPN FTFILDCNFK EALQRMQKRG NDNLLDEFIK GKNDFDTVRS YYLSLVDKKN CFLINGDNKQ EHLEKFIELL TRCLQQPTHY // ID KCY_MYCGE Reviewed; 217 AA. AC P47572; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 89. 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=MG330; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-179. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71554.1; -; Genomic_DNA. DR EMBL; U02241; AAA03397.1; -; Genomic_DNA. DR PIR; E64236; E64236. DR RefSeq; WP_010869435.1; NC_000908.2. DR ProteinModelPortal; P47572; -. DR STRING; 243273.MgenG_010200003205; -. DR EnsemblBacteria; AAC71554; AAC71554; MG_330. DR KEGG; mge:MG_330; -. DR PATRIC; 20010216; VBIMycGen98045_0385. DR eggNOG; ENOG4105CAT; Bacteria. DR eggNOG; COG0283; LUCA. DR KO; K00945; -. DR OMA; LKIFMTA; -. DR OrthoDB; EOG6Z6FZ4; -. DR BioCyc; MGEN243273:GH2R-378-MONOMER; -. DR Proteomes; UP000000807; 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 1 217 Cytidylate kinase. FT /FTId=PRO_0000131936. FT NP_BIND 9 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00238}. SQ SEQUENCE 217 AA; 24744 MW; 73FA658FB90156DD CRC64; MNWQIAIDGP SSSGKSSVAK KIAEELDFFY FSSGKMYRAF AYVMQVNRLN IDLFLKIINQ INWRFEKDAV YYNNADITTV ITTQSVANIA SKIAVDPNIR KIAVIKQQKL AENKNIVMDG RDIGTVVLKN AQLKFFLDAK VEIRAQRRLQ DMGISLSNEK KLKELIQELK QRDQIDSSRT ADPLKKAQDA IYLDTSELSF DAVVKQTLKE AKKVFKL // ID KITH_MYCGE Reviewed; 213 AA. AC P47280; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124}; DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124}; GN Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124}; OrderedLocusNames=MG034; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}. CC -!- SIMILARITY: Belongs to the thymidine kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00124}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71250.1; -; Genomic_DNA. DR PIR; G64203; G64203. DR RefSeq; WP_009885698.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47280; -. DR STRING; 243273.MgenG_010200000995; -. DR EnsemblBacteria; AAC71250; AAC71250; MG_034. DR KEGG; mge:MG_034; -. DR PATRIC; 20009444; VBIMycGen98045_0032. DR eggNOG; ENOG4107T8J; Bacteria. DR eggNOG; COG1435; LUCA. DR KO; K00857; -. DR OMA; KEQFGWI; -. DR OrthoDB; EOG69D3J2; -. DR BioCyc; MGEN243273:GH2R-34-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA synthesis; Kinase; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; KW Zinc. FT CHAIN 1 213 Thymidine kinase. FT /FTId=PRO_0000174994. FT NP_BIND 20 27 ATP. {ECO:0000255|HAMAP-Rule:MF_00124}. FT NP_BIND 93 96 ATP. {ECO:0000255|HAMAP-Rule:MF_00124}. FT ACT_SITE 94 94 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00124}. FT METAL 150 150 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 153 153 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 185 185 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 188 188 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. SQ SEQUENCE 213 AA; 24101 MW; 08E9C93CE4556326 CRC64; MGKYQPSFQT KKGWTEVICG PMFSGKTEKL LHKIKRWKIA KISVVIFKPI IDTRQTNIVK SRNGEYDQAI TINSPFEIYD HLVDKNYQIV AIDEAQFFSN EIIEVVTTLN EIGTNVIISG LDTDFRAEPF GCIPQLLAIA DVVNKLDAIC NVCGSLAQRT QRLVNKNTND NLVLIGDAEA YEARCKLHHS FLTKKHVTVK TKNFKEQVQG KTQ // ID KPRS_MYCGE Reviewed; 344 AA. AC P47304; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2002, sequence version 2. DT 13-APR-2016, entry version 106. 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}; Synonyms=prsA; GN OrderedLocusNames=MG058; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC71275.1; 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; L43967; AAC71275.1; ALT_INIT; Genomic_DNA. DR PIR; D64206; D64206. DR ProteinModelPortal; P47304; -. DR STRING; 243273.MgenG_010200001180; -. DR EnsemblBacteria; AAC71275; AAC71275; MG_058. DR KEGG; mge:MG_058; -. DR PATRIC; 20009498; VBIMycGen98045_0059. DR eggNOG; ENOG4105C5T; Bacteria. DR eggNOG; COG0462; LUCA. DR KO; K00948; -. DR OMA; GHPVSAR; -. DR OrthoDB; EOG6Z99XQ; -. DR BioCyc; MGEN243273:GH2R-60-MONOMER; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000000807; 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:0009116; P:nucleoside metabolic process; IEA:InterPro. 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; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005946; Rib-P_diPkinase. DR Pfam; PF00156; Pribosyltran; 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 1 344 Ribose-phosphate pyrophosphokinase. FT /FTId=PRO_0000141160. FT NP_BIND 55 57 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT NP_BIND 114 117 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 211 213 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 238 245 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 328 330 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT METAL 146 146 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 148 148 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 157 157 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 161 161 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 122 122 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 148 148 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 153 153 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 188 188 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 344 AA; 38881 MW; 41AFB21B36605DAD CRC64; MKLLKRKQSD ASLKLSIDNK KHVIFSLSKS KTLVENICKK LNISEGKMVC EHFADGETYI RFDESVRNKD IYIFQSTCPN VNDSLMELLI AIDALKRGSA KSITAILPYY GYARQDRKTK GREPITSKLI ADMLTKAGAN RVVLTDIHSD QTQGFFDIPV DSLRTYHIFL FRVIELLGKK DLVVVSPDYG GVKRARLIAN TLELPLAIID KRRPSHNVAE SINVLGEVKN KNCLIVDDMI DTGGTVIAAA KLLQKEQAKK VCVMATHGLF NNDAEQKFME AFDQKLIDFL FVSNSIPQYK FKAVKQFEVV DLASLYEEVV LCYANSLSVS AIYERHIEWI KKHV // ID KPYK_MYCGE Reviewed; 508 AA. AC P47458; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OrderedLocusNames=MG216; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 264-372. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC -!- ENZYME REGULATION: Regulated by phosphoenolpyruvate substrate and CC is allosterically activated by ribose-5-phosphate, AMP and other CC nucleoside monophosphates but not by fructose-1,6-bisphosphate. CC {ECO:0000250}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. 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; L43967; AAC71435.1; -; Genomic_DNA. DR EMBL; U01798; AAD12324.1; -; Genomic_DNA. DR PIR; H64223; H64223. DR RefSeq; WP_009885755.1; NZ_AAGX01000004.1. DR ProteinModelPortal; P47458; -. DR STRING; 243273.MgenG_010200001452; -. DR EnsemblBacteria; AAC71435; AAC71435; MG_216. DR KEGG; mge:MG_216; -. DR PATRIC; 20009892; VBIMycGen98045_0251. DR eggNOG; ENOG4105CA9; Bacteria. DR eggNOG; COG0469; LUCA. DR KO; K00873; -. DR OMA; ERPCAPI; -. DR OrthoDB; EOG6GBMB0; -. DR BioCyc; MGEN243273:GH2R-228-MONOMER; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000000807; 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; IPR018209; Pyrv_Knase_AS. DR InterPro; IPR015793; Pyrv_Knase_brl. DR InterPro; IPR015795; Pyrv_Knase_C. DR InterPro; IPR015806; Pyrv_Knase_insert_dom. DR PANTHER; PTHR11817; PTHR11817; 2. DR Pfam; PF00224; PK; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR SUPFAM; SSF50800; SSF50800; 1. DR SUPFAM; SSF51621; SSF51621; 2. DR SUPFAM; SSF52935; SSF52935; 2. DR TIGRFAMs; TIGR01064; pyruv_kin; 1. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Complete proteome; Glycolysis; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Potassium; Pyruvate; KW Reference proteome; Transferase. FT CHAIN 1 508 Pyruvate kinase. FT /FTId=PRO_0000112079. FT METAL 58 58 Potassium. {ECO:0000250}. FT METAL 60 60 Potassium. {ECO:0000250}. FT METAL 90 90 Potassium. {ECO:0000250}. FT METAL 91 91 Potassium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 251 251 Magnesium. {ECO:0000250}. FT METAL 275 275 Magnesium. {ECO:0000250}. FT BINDING 56 56 Substrate. {ECO:0000250}. FT BINDING 274 274 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 275 275 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 307 307 Substrate. {ECO:0000250}. FT SITE 249 249 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 508 AA; 57333 MW; E4C38BB0E92C5F8E CRC64; MIDHLKRTKI IATCGPALTK SLVSLKMLDD NEYAAIKKVA YANIEAIIKS GVSVIRLNFS HGTHEEQQVR IKIVRDVAKA MNIPVSIMLD TNGPEIRIVE TKKEGLKITK DSEVIINTMS KMIASDNQFA VSDASGKYNM VNDVNIGQKI LVDDGKLTLV VTRVDKQHNQ VICVAKNDHT VFTKKRLNLP NAQYSIPFLS EKDLKDIDFG LSQGIDYIAA SFVNTVADIK QLRDYLKLKN ASGVKIIAKI ESNHALNNID KIIKASDGIM VARGDLGLEI PYYQVPYWQR YMIKACRFFN KRSITATQML DSLEKNIQPT RAEVTDVYFA VDRGNDATML SGETASGLYP LNAVAVMQKI DKQSETFFDY QYNVNYYLKN STANKSRFWH NVVLPLTKKT VPKRKLVNSA FKYDFIVYPT NNINRIYALS NARLAAAVII LTNNKRVYTG HGVDYGIFCY LIDKNPNQLT KAELIELAWK AINHYQAYGD LEKLKQCLAV YNETIINL // ID LDH_MYCGE Reviewed; 312 AA. AC P47698; Q49200; Q59528; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=L-lactate dehydrogenase; DE Short=L-LDH; DE EC=1.1.1.27; GN Name=ldh; OrderedLocusNames=MG460; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC43202.1; 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; L43967; AAC72480.1; -; Genomic_DNA. DR EMBL; U01725; AAC43202.1; ALT_INIT; Unassigned_DNA. DR EMBL; U01708; AAB01020.1; ALT_SEQ; Genomic_DNA. DR PIR; H64250; H64250. DR RefSeq; WP_009885571.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47698; -. DR STRING; 243273.MgenG_010200000125; -. DR EnsemblBacteria; AAC72480; AAC72480; MG_460. DR KEGG; mge:MG_460; -. DR PATRIC; 20010514; VBIMycGen98045_0530. DR eggNOG; ENOG4105C80; Bacteria. DR eggNOG; COG0039; LUCA. DR KO; K00016; -. DR OMA; AGDYEDC; -. DR OrthoDB; EOG6091FG; -. DR BioCyc; MGEN243273:GH2R-513-MONOMER; -. DR UniPathway; UPA00554; UER00611. DR Proteomes; UP000000807; 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:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. 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; 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; KW Reference proteome. FT CHAIN 1 312 L-lactate dehydrogenase. FT /FTId=PRO_0000168368. FT NP_BIND 12 40 NAD. {ECO:0000250}. FT ACT_SITE 177 177 Proton acceptor. {ECO:0000250}. FT BINDING 90 90 Substrate. {ECO:0000250}. FT BINDING 122 122 NAD or substrate. {ECO:0000250}. FT BINDING 153 153 Substrate. {ECO:0000250}. FT BINDING 229 229 Substrate. {ECO:0000250}. FT MOD_RES 220 220 Phosphotyrosine. {ECO:0000250}. SQ SEQUENCE 312 AA; 33966 MW; D70E0BD04F75B984 CRC64; MKGPKIAIVG SGAVGTSFLY AAMTRALGSE YMIIDINEKA KVGNVFDLQD ASSSCPNFGK VVAGEYSQLK DYDFIFISAG RPQKQGGETR LQLLEGNVEI MKSIAKEIKK SGFNGVTLIA SNPVDIMSYT YLKVTGFEPN KVIGSGTLLD SARLRYAIAT KYQMSSKDVQ AYVIGEHGDS SVSIISSAKI AGLSLKHFSK ASDIEKEFGE IDQFIRRRAY EIIERKGATF YGIGEASADV AEQILKDTKE VRVVAPLLTG QYGAKDMMFG TPCVLSRKGI EKILEIELSN TEKVALENSI KVLKDNIKLA KL // ID LGT_MYCGE Reviewed; 382 AA. AC P47332; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Prolipoprotein diacylglyceryl transferase; DE EC=2.4.99.-; GN Name=lgt; OrderedLocusNames=MG086; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Transfers the N-acyl diglyceride group on what will CC become the N-terminal cysteine of membrane lipoproteins. CC {ECO:0000250}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis CC (diacylglyceryl transfer). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Lgt 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; L43967; AAC71304.1; -; Genomic_DNA. DR PIR; E64209; E64209. DR RefSeq; WP_009885643.1; NZ_AAGX01000002.1. DR STRING; 243273.MgenG_010200000650; -. DR PRIDE; P47332; -. DR EnsemblBacteria; AAC71304; AAC71304; MG_086. DR KEGG; mge:MG_086; -. DR PATRIC; 20009574; VBIMycGen98045_0096. DR eggNOG; ENOG4107TBN; Bacteria. DR eggNOG; COG0682; LUCA. DR KO; K13292; -. DR OMA; FFWRREK; -. DR OrthoDB; EOG690MBD; -. DR BioCyc; MGEN243273:GH2R-89-MONOMER; -. DR UniPathway; UPA00664; -. DR Proteomes; UP000000807; 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; 2. DR TIGRFAMs; TIGR00544; lgt; 1. DR PROSITE; PS01311; LGT; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 382 Prolipoprotein diacylglyceryl FT transferase. FT /FTId=PRO_0000172633. FT TRANSMEM 20 42 Helical. {ECO:0000255}. FT TRANSMEM 49 71 Helical. {ECO:0000255}. FT TRANSMEM 91 113 Helical. {ECO:0000255}. FT TRANSMEM 215 234 Helical. {ECO:0000255}. FT TRANSMEM 244 261 Helical. {ECO:0000255}. FT TRANSMEM 274 296 Helical. {ECO:0000255}. FT TRANSMEM 301 323 Helical. {ECO:0000255}. SQ SEQUENCE 382 AA; 44431 MW; 427E37B5B5C3806F CRC64; MNRPSWSTAF NIGGGFPIQW YGIIVSIGII FAILMFVFKL IYCYKLQDNS FYFFIFIAVL TMVLGARLWS FVIGDSNFAN NNFFDFRNGG LAIQGGILLT SIVGVIYFNF FLNSKTNKTK TIAELLNNKN EIKAVYVERN ISVLVMLDLI APCVLIGQAI GRWGNFFNQE VYGFALAGTM NDPQALANTQ WGFLKILMPK VWDGMWIDGQ FRIPLFLIES FFNTIFFVLI YFVMDFIRGV KSGTIGFSYF LATGIIRLIL ENFRDQTFYF QTSITTSILF IVVGILGIFY CQFIHVKLRN YFWTYFFLYA FYKVAAFFTT LFLNNRKQMA QQKFAFYEKS LPNKKRSFFE MKYYNDVTTP KIYRLTDQEM KLFDKLEAVT TS // ID LEPA_MYCGE Reviewed; 598 AA. AC P47384; Q49264; Q49477; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 109. 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}; OrderedLocusNames=MG138; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-197. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-413 AND 440-598. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 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; L43967; AAC71355.1; -; Genomic_DNA. DR EMBL; X61521; CAB97511.1; -; Genomic_DNA. DR EMBL; U01745; AAD10558.1; -; Genomic_DNA. DR EMBL; U02133; AAD12410.1; -; Genomic_DNA. DR PIR; C64215; C64215. DR RefSeq; WP_010869350.1; NC_000908.2. DR ProteinModelPortal; P47384; -. DR EnsemblBacteria; AAC71355; AAC71355; MG_138. DR KEGG; mge:MG_138; -. DR PATRIC; 20009682; VBIMycGen98045_0150. DR KO; K03596; -. DR OMA; KPMVFCG; -. DR OrthoDB; EOG6ZKXQ4; -. DR BioCyc; MGEN243273:GH2R-142-MONOMER; -. DR Proteomes; UP000000807; Chromosome. 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: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 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; IPR031157; G_TR_CS. 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 SMART; SM00838; EFG_C; 1. 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; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; GTP-binding; Hydrolase; Membrane; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 598 Elongation factor 4. FT /FTId=PRO_0000176298. FT DOMAIN 4 185 tr-type G. FT NP_BIND 16 21 GTP. {ECO:0000255|HAMAP-Rule:MF_00071}. FT NP_BIND 132 135 GTP. {ECO:0000255|HAMAP-Rule:MF_00071}. FT CONFLICT 413 413 D -> G (in Ref. 3; AAD12410). FT {ECO:0000305}. SQ SEQUENCE 598 AA; 67937 MW; C16F1864E24C941D CRC64; MEQKNIRNFS IIAHIDHGKS TLSDRLLEHS LGFEKRLLQA QMLDTMEIER ERGITIKLNA VELKINVDNN NYLFHLIDTP GHVDFTYEVS RSLAACEGVL LLVDATQGIQ AQTISNAYLA LENNLEIIPV INKIDMDNAD IETTKDSLHN LLGVEKNSIC LVSAKANLGI DQLIQTIIAK IPPPKGEINR PLKALLFDSY YDPYKGVVCF IRVFDGCLKV NDKVRFIKSN SVYQIVELGV KTPFFEKRDQ LQAGDVGWFS AGIKKLRDVG VGDTIVSFDD QFTKPLAGYK KILPMIYCGL YPVDNSDYQN LKLAMEKIII SDAALEYEYE TSQALGFGVR CGFLGLLHMD VIKERLEREY NLKLISAPPS VVYKVLLTNG KEISIDNPSL LPERSKIKAI SEPFVKVFID LPDQYLGSVI DLCQNFRGQY ESLNEIDINR KRICYLMPLG EIIYSFFDKL KSISKGYASL NYEFYNYQHS QLEKVEIMLN KQKIDALSFI SHKDFAFKRA KKFCTKLKEL IPKHLFEIPI QATIGSKVIA RETIKAVRKD VIAKLYGGDV SRKKKLLEKQ KEGKKRLKAV GSVQLPQELF SHLLKDED // ID LSPA_MYCGE Reviewed; 181 AA. AC Q49401; Q49210; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Lipoprotein signal peptidase; DE EC=3.4.23.36; DE AltName: Full=Prolipoprotein signal peptidase; DE AltName: Full=Signal peptidase II; DE Short=SPase II; GN Name=lspA; Synonyms=lsp; OrderedLocusNames=MG210; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: This protein specifically catalyzes the removal of CC signal peptides from prolipoproteins. {ECO:0000250}. 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. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal CC peptide cleavage). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase A8 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; L43967; AAC71428.1; -; Genomic_DNA. DR EMBL; U01759; AAD10573.1; -; Genomic_DNA. DR PIR; B64223; B64223. DR RefSeq; WP_009885747.1; NZ_AAGX01000004.1. DR STRING; 243273.MgenG_010200001402; -. DR EnsemblBacteria; AAC71428; AAC71428; MG_210. DR KEGG; mge:MG_210; -. DR PATRIC; 20009874; VBIMycGen98045_0242. DR eggNOG; COG0597; LUCA. DR KO; K03101; -. DR OMA; FINIYVI; -. DR OrthoDB; EOG647V1T; -. DR BioCyc; MGEN243273:GH2R-219-MONOMER; -. DR UniPathway; UPA00665; -. DR Proteomes; UP000000807; 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 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; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Protease; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 181 Lipoprotein signal peptidase. FT /FTId=PRO_0000178794. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 149 169 Helical. {ECO:0000255}. FT ACT_SITE 127 127 {ECO:0000250}. FT ACT_SITE 153 153 {ECO:0000250}. SQ SEQUENCE 181 AA; 20841 MW; FF3225CF9E42B9C9 CRC64; MKLRKTKFFS QLKHQVLTAN QKPFLFYKLT MIGFVGFIIL LQVFILRNAL NGEMDNTMVA NSGFINIYVI RNKGVGFSLL QNQTGLVYFL QGLLSVIALV FLVFMVKYSY IFWITTLAFG SLGNFFDRLT SANDSVLDYF IFQNGSSVFN FADCCITFGF IGLFFCFLIQ MFKEFKHSKN Q // ID LON_MYCGE Reviewed; 795 AA. AC P47481; Q49276; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=Lon protease {ECO:0000255|HAMAP-Rule:MF_01973}; DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973}; DE AltName: Full=ATP-dependent protease La {ECO:0000255|HAMAP-Rule:MF_01973}; GN Name=lon {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=MG239; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 484-606. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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:0000255|HAMAP-Rule:MF_01973}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP. CC {ECO:0000255|HAMAP-Rule:MF_01973}. CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. CC {ECO:0000255|HAMAP-Rule:MF_01973}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}. CC -!- SIMILARITY: Belongs to the peptidase S16 family. CC {ECO:0000255|HAMAP-Rule:MF_01973}. CC -!- SIMILARITY: Contains 1 Lon N-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU01123}. CC -!- SIMILARITY: Contains 1 Lon proteolytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU01122}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71460.1; -; Genomic_DNA. DR EMBL; U02148; AAD12428.1; -; Genomic_DNA. DR PIR; D64226; D64226. DR RefSeq; WP_009885776.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47481; -. DR STRING; 243273.MgenG_010200001622; -. DR MEROPS; S16.004; -. DR EnsemblBacteria; AAC71460; AAC71460; MG_239. DR KEGG; mge:MG_239; -. DR PATRIC; 20009960; VBIMycGen98045_0276. DR eggNOG; ENOG4105C6P; Bacteria. DR eggNOG; COG0466; LUCA. DR KO; K01338; -. DR OMA; EGTFMPG; -. DR OrthoDB; EOG6XHC23; -. DR BioCyc; MGEN243273:GH2R-261-MONOMER; -. DR Proteomes; UP000000807; 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; PS51787; LON_N; 1. DR PROSITE; PS51786; LON_PROTEOLYTIC; 1. DR PROSITE; PS01046; LON_SER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Hydrolase; KW Nucleotide-binding; Protease; Reference proteome; Serine protease; KW Stress response. FT CHAIN 1 795 Lon protease. FT /FTId=PRO_0000076139. FT DOMAIN 7 211 Lon N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU01123}. FT DOMAIN 615 795 Lon proteolytic. {ECO:0000255|PROSITE- FT ProRule:PRU01122}. FT NP_BIND 379 386 ATP. {ECO:0000255|HAMAP-Rule:MF_01973}. FT COMPBIAS 304 308 Poly-Ser. FT ACT_SITE 702 702 {ECO:0000255|HAMAP-Rule:MF_01973}. FT ACT_SITE 745 745 {ECO:0000255|HAMAP-Rule:MF_01973}. FT CONFLICT 494 494 T -> S (in Ref. 2; AAD12428). FT {ECO:0000305}. SQ SEQUENCE 795 AA; 89988 MW; 31C8188EA40F5E39 CRC64; MPVTKKSQIL VVRGQVIFPF VPFSLDVGRP RSRKIIKALK TLKTKRLVLV TQKFTGEQNP EFNDIYHVGT LCEIDEIVDV PGVDSKTVDY RIKGRGLQRV LIEKFSDADI NEVSYQLLNS TVKDEANVDR FLQRIFPEKE EIEQLMEGAE KFLELENISK TVNVPKGLKQ LDIITFKLAN LVPNTESIKQ AILEENEIAN RLEKIIQAGI EDLQKIQDYG RSKNKETEFD KLDSKITRKI NEQLSRQQRD FYLREKLRII REEIGISSKK EDEVASIRKK LDENPYPEAI KKRILSELEH YENSSSSSQE STLTKTYIDT LLNLPWWQKS KDNSDVKNLI KTLDKNHTGL DKVKERIVEY LAVQLRTQKN KGPIMCLVGP PGVGKSSLAK SIAEALDKKF VKISLGGVHD ESEIRGHRKT YLGSMPGRIL KGMTRAKVIN PLFLLDEIDK MTSSNQGYPS GALLEVLDPE LNNKFSDNYV EEDYDLSKVM FIATANYIED IPEALLDRME IIELTSYTEQ EKIEIAKNHL IKRCLEDADL NSEELKFTDE AISYIIKFYT REAGVRQLER LIQQVVRKYI VAMQKDGIKQ ETIDVNAVKK YLKKEIFDHT MRDEVSLPGI VNGMAYTPTG GDLLPIEVTH VAGKGELILT GNLKQTMRES ANVALGYVKA NAERFNINPS LFKKIDINIH VPGGGIPKDG PSAGAALVTA IISSLTGKKV DPTVAMTGEI TLRGKVLVIG GVKEKTISAY RGGVTTIFMP EKNERYLDEV PKEIVDKLNI IFVKEYSDIY NKLFS // ID LPLA_MYCGE Reviewed; 336 AA. AC P47512; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Probable lipoate-protein ligase A; DE Short=Lipoate--protein ligase; DE EC=6.3.1.20; GN Name=lplA; OrderedLocusNames=MG270; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Catalyzes both the ATP-dependent activation of CC exogenously supplied lipoate to lipoyl-AMP and the transfer of the CC activated lipoyl onto the lipoyl domains of lipoate-dependent CC enzymes. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + (R)-lipoate + a [lipoyl-carrier CC protein]-L-lysine = a [lipoyl-carrier protein]-N(6)-(lipoyl)lysine CC + AMP + diphosphate. CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2. CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group CC of lipoic acid is attached via an amide linkage to the epsilon- CC amino group of a specific lysine residue of lipoyl domains of CC lipoate-dependent enzymes. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LplA family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 BPL/LPL catalytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU01067}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71492.1; -; Genomic_DNA. DR PIR; H64229; H64229. DR RefSeq; WP_009885902.1; NZ_AAGX01000009.1. DR ProteinModelPortal; P47512; -. DR STRING; 243273.MgenG_010200002634; -. DR EnsemblBacteria; AAC71492; AAC71492; MG_270. DR KEGG; mge:MG_270; -. DR PATRIC; 20010040; VBIMycGen98045_0312. DR eggNOG; ENOG4107UFM; Bacteria. DR eggNOG; COG0095; LUCA. DR KO; K03800; -. DR OMA; WRNAETV; -. DR OrthoDB; EOG6038ZS; -. DR BioCyc; MGEN243273:GH2R-298-MONOMER; -. DR UniPathway; UPA00537; UER00594. DR UniPathway; UPA00537; UER00595. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009249; P:protein lipoylation; IEA:InterPro. DR InterPro; IPR004143; BPL_LPL_catalytic. DR InterPro; IPR019491; Lipoate_protein_ligase_C. DR InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase. DR Pfam; PF03099; BPL_LplA_LipB; 1. DR Pfam; PF10437; Lip_prot_lig_C; 1. DR TIGRFAMs; TIGR00545; lipoyltrans; 1. DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 336 Probable lipoate-protein ligase A. FT /FTId=PRO_0000209567. FT DOMAIN 30 217 BPL/LPL catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU01067}. FT NP_BIND 77 80 ATP. {ECO:0000250}. FT BINDING 72 72 ATP. {ECO:0000250}. FT BINDING 135 135 ATP. {ECO:0000250}. FT BINDING 135 135 Lipoate. {ECO:0000250}. SQ SEQUENCE 336 AA; 38944 MW; 9804256E786E1E9C CRC64; MQTFIITSPV FNPYFNAALE EWLLTEFRKN ELVKVIYFWQ NANTIVVGRN QNTYAEVNLK ELESDKVNLF RRFSGGGAVF HDLGNICFSI ILPRTGKVME NAYEQTTRNV VKFLNSLNVP AVFHGRNDLE INNKKFSGLA EYIAKDRLLV HGTLLFDTDF SKLAKYLNVD KTKIASKGVD SVAKRVVNVK EYLPNWTTAK FLEEMINFFT VTEKAETIVL TKDALAKVEK RAKEHFQSWE WNFGKTYEYN FKNKRYFNNA GLFECNVQVE KGTVVDIKFY GDFLSVVDIT PVTKKLIGQK YDYKTFEKLF NELDHFSDYF GSLKPEQLLG VIFDNK // ID MANB_MYCGE Reviewed; 550 AA. AC P47299; Q49247; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Phosphomannomutase; DE Short=PMM; DE EC=5.4.2.8; GN Name=manB; Synonyms=cpsG; OrderedLocusNames=MG053; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: Alpha-D-mannose 1-phosphate = D-mannose 6- CC 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 -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD12379.1; 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; L43967; AAC71269.1; -; Genomic_DNA. DR EMBL; U02108; AAD12379.1; ALT_INIT; Genomic_DNA. DR PIR; H64205; H64205. DR RefSeq; WP_009885715.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47299; -. DR STRING; 243273.MgenG_010200001140; -. DR EnsemblBacteria; AAC71269; AAC71269; MG_053. DR KEGG; mge:MG_053; -. DR PATRIC; 20009486; VBIMycGen98045_0053. DR eggNOG; ENOG4107QSU; Bacteria. DR eggNOG; COG1109; LUCA. DR KO; K01840; -. DR OMA; QAGSMGM; -. DR OrthoDB; EOG6103ZG; -. DR BioCyc; MGEN243273:GH2R-53-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. 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; Isomerase; Magnesium; Metal-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1 550 Phosphomannomutase. FT /FTId=PRO_0000147828. FT ACT_SITE 148 148 Phosphoserine intermediate. FT {ECO:0000250}. FT METAL 148 148 Magnesium; via phosphate group. FT {ECO:0000250}. FT METAL 300 300 Magnesium. {ECO:0000250}. FT METAL 302 302 Magnesium. {ECO:0000250}. FT METAL 304 304 Magnesium. {ECO:0000250}. FT CONFLICT 42 46 PLFGT -> LYLAL (in Ref. 2; AAD12379). FT {ECO:0000305}. SQ SEQUENCE 550 AA; 63397 MW; D7BDF8920923508D CRC64; MDKLRLEVER WLNHPNVNWE LKQQIKELNE SEIQELFSLE KPLFGTAGVR NKMAPGYHGM NVFSYAYLTQ GYVKYIESIN EPKRQLRFLV ARDTRKNGGL FLETVCDVIT SMGHLAYVFD DNQPVSTPLV SHVIFKYGFS GGINITASHN PKDDNGFKVY DHTGAQLLDT QTNQLLSDLP CVTSMLDLEL QPNPKFVHTL DNEKVYKNYF RELKKVLVIN NNNFKDIKVV FSGLNGTSVC LMQRFLKYLG YSNIISVEEQ NWFDENFENA PNLNPEYKDT WILAQKYAKK NNAKLIIMAD PDADRFAIAE LNNNQWHYFS GNETGAITAY YKLNHKVFKS PYIVSTFVST YLVNKIAKRY GAFVHRTNVG FKYIGQAINE LSQTNELVVG FEEAIGLITS DKLNREKDAY QAAALLLEIA RHCKEQNITL LDFYKRILSE FGEYFNLTIS HPFKATATDW KEEIKALFNQ LINANLTEVA GFKVVKVHLD KQTNILEFGF ENGWVKFRFS GTEPKLKFYF DLTNGTREAL EKQAKKIYKF FVNLLKLNKA // ID MAP1_MYCGE Reviewed; 248 AA. AC P47418; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Methionine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_01974}; DE Short=MAP {ECO:0000255|HAMAP-Rule:MF_01974}; DE Short=MetAP {ECO:0000255|HAMAP-Rule:MF_01974}; DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_01974}; DE AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_01974}; GN Name=map {ECO:0000255|HAMAP-Rule:MF_01974}; OrderedLocusNames=MG172; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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:0000255|HAMAP-Rule:MF_01974}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids, CC preferentially methionine, from peptides and arylamides. CC {ECO:0000255|HAMAP-Rule:MF_01974}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000255|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:0000255|HAMAP- CC Rule:MF_01974}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01974}. CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase type 1 subfamily. {ECO:0000255|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; L43967; AAC71390.1; -; Genomic_DNA. DR PIR; A64219; A64219. DR RefSeq; WP_009885857.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47418; -. DR STRING; 243273.MgenG_010200002264; -. DR EnsemblBacteria; AAC71390; AAC71390; MG_172. DR KEGG; mge:MG_172; -. DR PATRIC; 20009776; VBIMycGen98045_0194. DR eggNOG; ENOG4105CA1; Bacteria. DR eggNOG; COG0024; LUCA. DR KO; K01265; -. DR OMA; PNFGKAG; -. DR OrthoDB; EOG6MWNDS; -. DR BioCyc; MGEN243273:GH2R-181-MONOMER; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW Aminopeptidase; Complete proteome; Hydrolase; Metal-binding; Protease; KW Reference proteome. FT CHAIN 1 248 Methionine aminopeptidase. FT /FTId=PRO_0000148946. FT METAL 94 94 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 105 105 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 105 105 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 169 169 Divalent metal cation 2; catalytic; via FT tele nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01974}. FT METAL 202 202 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 233 233 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 233 233 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT BINDING 77 77 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01974}. FT BINDING 176 176 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01974}. SQ SEQUENCE 248 AA; 27738 MW; EE3E965632AD7E76 CRC64; MIYLKSANEV AGIKKACAIF KAVKAYFTIE KLLGKKLVTI DRLIKQFIEQ KQAKCAFHGY LGFPGFNCLS LNQTVIHGVA DQTVFKDSDK LTLDIGIDYH GYLCDAAFTL LGNKADPKAV KLLNDVEQAF SKVIEPELFV NNPIGNLSNA IQTYFENKGY FLVKEFGGHG CGIKIHEDPL ILNWGEKNQG VRLQEGMVIC IEPMVMTDSS EITMAANNWN VLTLKSKFNC HVEQMYHITN NGFECLTN // ID METK_MYCGE Reviewed; 383 AA. AC P47293; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 111. 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; Synonyms=metX; OrderedLocusNames=MG047; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-357. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71263.1; -; Genomic_DNA. DR EMBL; U02123; AAD12398.1; -; Genomic_DNA. DR PIR; B64205; B64205. DR RefSeq; WP_009885709.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47293; -. DR STRING; 243273.MgenG_010200001100; -. DR EnsemblBacteria; AAC71263; AAC71263; MG_047. DR KEGG; mge:MG_047; -. DR PATRIC; 20009472; VBIMycGen98045_0046. DR eggNOG; ENOG4105CPH; Bacteria. DR eggNOG; COG0192; LUCA. DR KO; K00789; -. DR OMA; DNFLAFD; -. DR OrthoDB; EOG68WR6M; -. DR BioCyc; MGEN243273:GH2R-47-MONOMER; -. DR UniPathway; UPA00315; UER00080. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-HAMAP. 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 1 383 S-adenosylmethionine synthase. FT /FTId=PRO_0000174550. FT NP_BIND 256 263 ATP. {ECO:0000255}. FT METAL 24 24 Magnesium. {ECO:0000250}. FT METAL 50 50 Potassium. {ECO:0000250}. FT METAL 260 260 Potassium. {ECO:0000250}. FT METAL 268 268 Magnesium. {ECO:0000250}. SQ SEQUENCE 383 AA; 42716 MW; F2340734FAA9EE16 CRC64; MAIRIKSTRV GRFVSESVGL GHPDKICDQI ADSILDQCLL QSKTSHVACE VFASKNLILI GGEISTSGYV DVVQTAWRIL RNLGYNETDF SFLSCINNQS LEINQAVLKN NEINAGDQGI TVGYAVNETK QLMPLGVLLA HSFLKQAEKL TKQFDFLKND MKSQVVLNYS LNQVECEEVL LSIQHTNAIS LTELRKVIEN NVILPVLNQY GFQDKKPTCL VNPGGSFVLG GPMADTGLTG RKIIVDTYGP YAHHGGGSFS GKDPSKVDRT GAYFARFIAK HIVSLGWASE CEVSISWVFS KPNPQSITVK CFNTNIQYDE VLINRVVNNY FNWSITKIID KLKLLDFVKY SDYAVYGHFG NDLSPWEQPT ELDKLECLIK NFH // ID MGP3_MYCGE Reviewed; 1052 AA. AC P22747; Q49257; Q49284; Q49385; Q49481; Q49482; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=Mgp-operon protein 3; DE Short=Mgp3; DE AltName: Full=ORF-3 protein; DE Flags: Precursor; GN OrderedLocusNames=MG192; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=2583522; DOI=10.1016/0378-1119(89)90051-6; RA Inamine J.M., Loechel S., Collier A.M., Barile M.F., Hu P.-C.; RT "Nucleotide sequence of the MgPa (mgp) operon of Mycoplasma genitalium RT and comparison to the P1 (mpp) operon of Mycoplasma pneumoniae."; RL Gene 82:259-267(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-133; 260-370; 441-512; 769-902 RP AND 964-1052. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 769-964. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-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; M31431; AAA25421.1; -; Genomic_DNA. DR EMBL; L43967; AAC71411.1; -; Genomic_DNA. DR EMBL; U02124; AAD12399.1; -; Genomic_DNA. DR EMBL; U02161; AAD12443.1; -; Genomic_DNA. DR EMBL; U34967; AAA88890.1; -; Genomic_DNA. DR EMBL; U02157; AAD12439.1; -; Genomic_DNA. DR EMBL; U34970; AAA88899.1; -; Genomic_DNA. DR EMBL; X61525; CAB98130.1; -; Genomic_DNA. DR EMBL; X61527; CAB98131.1; -; Genomic_DNA. DR PIR; C64221; C64221. DR STRING; 243273.MgenG_010200003383; -. DR EnsemblBacteria; AAC71411; AAC71411; MG_192. DR KEGG; mge:MG_192; -. DR PATRIC; 20009828; VBIMycGen98045_0220. DR OrthoDB; EOG6H7FQG; -. DR BioCyc; MGEN243273:GH2R-201-MONOMER; -. DR Proteomes; UP000000807; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR InterPro; IPR007885; Mycoplasma_attach_MgpC. DR Pfam; PF05220; MgpC; 1. PE 3: Inferred from homology; KW Cell adhesion; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 39 {ECO:0000255}. FT CHAIN 40 1052 Mgp-operon protein 3. FT /FTId=PRO_0000021720. FT TRANSMEM 945 965 Helical. {ECO:0000255}. FT CONFLICT 60 68 LDSSYQIAD -> MIKPLPLLS (in Ref. 3; FT AAD12399). {ECO:0000305}. FT CONFLICT 125 126 TM -> SV (in Ref. 3; AAD12399). FT {ECO:0000305}. FT CONFLICT 474 481 TNNGTTGP -> SNQISSGT (in Ref. 3; FT AAD12439). {ECO:0000305}. FT CONFLICT 476 476 N -> S (in Ref. 3; AAA88890). FT {ECO:0000305}. FT CONFLICT 897 902 SVSPRI -> MSHQVS (in Ref. 3; CAB98131). FT {ECO:0000305}. SQ SEQUENCE 1052 AA; 114361 MW; F6C6D3B3D7789145 CRC64; MKTMRKQIYK KAYWLLLPFL PLALANTFLV KEDSKNVTAY TPFATPITDS KSDLVSLAQL DSSYQIADQT IHNTNLFVLF KSRDVKVKYE SSGSNNISFD STSQGEKPSY VVEFTNSTNI GIKWTMVKKY QLDVPNVSSD MNQVLKNLIL EQPLTKYTLN SSLAKEKGKT QREVHLGSGQ ANQWTSQRNQ HDLNNNPSPN ASTGFKLTTG NAYRKLSESW PIYEPIDGTK QGKGKDSSGW SSTEENEAKN DAPSVSGGGS SSGTFNKYLN TKQALESIGI LFDDQTPRNV ITQLYYASTS KLAVTNNHIV VMGNSFLPSM WYWVVERSAQ ENASNKPTWF ANTNLDWGED KQKQFVENQL GYKETTSTNS HNFHSKSFTQ PAYLISGIDS VNDQIIFSGF KAGSVGYDSS SSSSSSSSST KDQALAWSTT TSLDSKTGYK DLVTNDTGLN GPINGSFSIQ DTFSFVVPYS GNHTNNGTTG PIKTAYPVKK DQKSTVKINS LINATPLNSY GDEGIGVFDA LGLNYNFKSN QERLPSRTDQ IFVYGIVSPN ELRSAKSSAD STGSDTKVNW SNTQSRYLPV PYNYSEGIID ADGFKRPENR GASVTTFSGL KSIAPDGFAN SIANFSVGLK AGIDPNPVMS GKKANYGAVV LTRGGVVRLN FNPGNDSLLS TTDNNIAPIS FSFTPFTAAE SAVDLTTFKE VTYNQESGLW SYIFDSSLKP SHDGKQTPVT DNMGFSVITV SRTGIELNQD QATTTLDVAP SALAVQSGIQ STTQTLTGVL PLSEEFSAVI AKDSDQNKID IYKNNNGLFE IDTQLSNSVA TNNGGLAPSY TENRVDAWGK VEFADNSVLQ ARNLVDKTVD EIINTPEILN SFFRFTPAFE DQKATLVATK QSDTSLSVSP RIQFLDGNFY DLNSTIAGVP LNIGFPSRVF AGFAALPAWV IPVSVGSSVG ILFILLVLGL GIGIPMYRVR KLQDASFVNV FKKVDTLTTA VGSVYKKIIT QTGVVKKAPS ALKAANPSVK KPAAFLKPPV QPPSKPEGEQ KAVEVKSEET KS // ID MNME_MYCGE Reviewed; 442 AA. AC P47254; Q49330; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=tRNA modification GTPase MnmE {ECO:0000255|HAMAP-Rule:MF_00379}; DE EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_00379}; GN Name=mnmE {ECO:0000255|HAMAP-Rule:MF_00379}; GN Synonyms=thdF {ECO:0000255|HAMAP-Rule:MF_00379}, GN trmE {ECO:0000255|HAMAP-Rule:MF_00379}; OrderedLocusNames=MG008; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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. {ECO:0000255|HAMAP-Rule:MF_00379}. 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 -!- SEQUENCE CAUTION: CC Sequence=AAD12512.1; 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; L43967; AAC71224.1; -; Genomic_DNA. DR EMBL; U02216; AAD12512.1; ALT_INIT; Genomic_DNA. DR PIR; H64200; H64200. DR RefSeq; WP_010869287.1; NC_000908.2. DR ProteinModelPortal; P47254; -. DR STRING; 243273.MgenG_010200003181; -. DR EnsemblBacteria; AAC71224; AAC71224; MG_008. DR KEGG; mge:MG_008; -. DR PATRIC; 20009392; VBIMycGen98045_0008. DR eggNOG; ENOG4105C1H; Bacteria. DR eggNOG; COG0486; LUCA. DR KO; K03650; -. DR OMA; LIEISCH; -. DR OrthoDB; EOG6DC6K1; -. DR BioCyc; MGEN243273:GH2R-8-MONOMER; -. DR Proteomes; UP000000807; 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; 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 SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51709; G_TRME; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium; KW Metal-binding; Nucleotide-binding; Potassium; Reference proteome; KW tRNA processing. FT CHAIN 1 442 tRNA modification GTPase MnmE. FT /FTId=PRO_0000188891. FT DOMAIN 217 363 TrmE-type G. FT NP_BIND 227 232 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 246 252 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 271 274 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 227 227 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 231 231 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 246 246 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 248 248 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 251 251 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 252 252 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT BINDING 23 23 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 82 82 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 121 121 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 442 442 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. SQ SEQUENCE 442 AA; 50806 MW; C6D50D3274B0EB32 CRC64; MKSEINIFAL ATAPFNSALH IIRFSGPDVY EILNKITNKK ITRKGMQIQR TWIVDENNKR IDDVLLFKFV SPNSYTGEDL IEISCHGNML IVNEICALLL KKGGVYAKPG EFTQRSFLNG KMSLQQASAV NKLILSPNLL VKDIVLNNLA GEMDQQLEQI AQQVNQLVMQ MEVNIDYPEY LDEQVELSTL NNKVKLIIEK LKRIIENSKQ LKKLHDPFKI AIIGETNVGK SSLLNALLNQ DKAIVSNIKG STRDVVEGDF NLNGYLIKIL DTAGIRKHKS GLEKAGIKKS FESIKQANLV IYLLDATHPK KDLELISFFK KNKKDFFVFY NKKDLITNKF ENSISAKQKD IKELVDLLTK YINEFYKKID QKIYLIENWQ QILIEKIKEQ LEQFLKQQKK YLFFDVLVTH LREAQQDILK LLGKDVGFDL VNEIFNNFCL GK // ID MNMA_MYCGE Reviewed; 367 AA. AC P47537; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 99. 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=MG295; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71516.1; -; Genomic_DNA. DR PIR; F64232; F64232. DR RefSeq; WP_010869415.1; NC_000908.2. DR ProteinModelPortal; P47537; -. DR EnsemblBacteria; AAC71516; AAC71516; MG_295. DR KEGG; mge:MG_295; -. DR PATRIC; 20010120; VBIMycGen98045_0346. DR KO; K00566; -. DR OMA; CYYLKIW; -. DR OrthoDB; EOG6RZB5H; -. DR BioCyc; MGEN243273:GH2R-331-MONOMER; -. DR Proteomes; UP000000807; 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:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP. 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 1 367 tRNA-specific 2-thiouridylase MnmA. FT /FTId=PRO_0000121651. FT NP_BIND 11 18 ATP. {ECO:0000255|HAMAP-Rule:MF_00144}. FT REGION 109 111 Interaction with target base in tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT REGION 161 163 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT ACT_SITE 114 114 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00144}. FT ACT_SITE 211 211 Cysteine persulfide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT BINDING 37 37 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00144}. FT BINDING 139 139 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT SITE 140 140 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT SITE 350 350 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT DISULFID 114 211 Alternate. {ECO:0000255|HAMAP- FT Rule:MF_00144}. SQ SEQUENCE 367 AA; 41888 MW; F8C6409D8C2D0625 CRC64; MSIIAKTVFI GLSGGVDSAV SALLLKKQYQ EVIGVFMECW DETLNNDFYG HKKINNNKSG CSSFQDFQQA KKIANSLGIK LIKKNLIEAY WNKVFLPMIQ SFKKGLTPNP DIWCNRFIKF GLLHDFCKQI NPNSLFATGH YAKINMIENQ PLLSIPKDTN KDQTYFLANV KKEQFQNVIF PLADLKKITV RNIARENNWE VADKKDSTGI CFIGERHFSD FLKNYLPVKK GLIKDWKTKQ TISEHDGVWF YTIGQRSGLN LGGLKQRHFV VAKDIETNEL FVSCDKEELL KTTILLDQFN WLYTPKQLPS QVLVRIRHAQ KPEIAKLKLL SDNKLEITFK NPVISVASGQ FGVLYTLDQI CLGAGLI // ID MSRA_MYCGE Reviewed; 157 AA. AC P47648; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=Peptide methionine sulfoxide reductase MsrA; DE Short=Protein-methionine-S-oxide reductase; DE EC=1.8.4.11; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase; DE Short=Peptide Met(O) reductase; GN Name=msrA; Synonyms=pmsR; OrderedLocusNames=MG408; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP POSSIBLE FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=11544227; DOI=10.1128/JB.183.19.5645-5650.2001; RA Dhandayuthapani S., Blaylock M.W., Bebear C.M., Rasmussen W.G., RA Baseman J.B.; RT "Peptide methionine sulfoxide reductase (MsrA) is a virulence RT determinant in Mycoplasma genitalium."; RL J. Bacteriol. 183:5645-5650(2001). CC -!- FUNCTION: Has an important function as a repair enzyme for CC proteins that have been inactivated by oxidation. Catalyzes the CC reversible oxidation-reduction of methionine sulfoxide in proteins CC to methionine (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O = CC L-methionine (S)-S-oxide + thioredoxin. CC -!- DISRUPTION PHENOTYPE: Decreased agglutination to sheep CC erythrocytes and survival in hamster lungs and increased CC sensitivity to hydrogen peroxide. {ECO:0000269|PubMed:11544227}. CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase 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; L43967; AAC71636.1; -; Genomic_DNA. DR PIR; B64245; B64245. DR RefSeq; WP_010869470.1; NC_000908.2. DR ProteinModelPortal; P47648; -. DR STRING; 243273.MgenG_010200000450; -. DR EnsemblBacteria; AAC71636; AAC71636; MG_408. DR KEGG; mge:MG_408; -. DR PATRIC; 20010408; VBIMycGen98045_0477. DR eggNOG; ENOG4108HW8; Bacteria. DR eggNOG; COG0225; LUCA. DR KO; K07304; -. DR OMA; TYEDICT; -. DR OrthoDB; EOG6091JX; -. DR BioCyc; MGEN243273:GH2R-465-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006464; P:cellular protein modification process; IEA:UniProtKB-HAMAP. DR GO; GO:0030091; P:protein repair; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.30.1060.10; -; 1. DR HAMAP; MF_01401; MsrA; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA. DR PANTHER; PTHR10173; PTHR10173; 1. DR Pfam; PF01625; PMSR; 1. DR SUPFAM; SSF55068; SSF55068; 1. DR TIGRFAMs; TIGR00401; msrA; 1. PE 1: Evidence at protein level; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 157 Peptide methionine sulfoxide reductase FT MsrA. FT /FTId=PRO_0000138556. FT ACT_SITE 10 10 {ECO:0000250}. SQ SEQUENCE 157 AA; 18415 MW; 1938A53365982705 CRC64; MKEIYFGGGC FWGIEKYFQL IKGVKKTSVG YLNSRIRNPS YEQVCSGYTN AVEAVKVEYE EKEISLSELI EALFEVIDPT IRNRQGNDIG TQYRTGIYWT DSSDEKIIND KFLKLQKNYS KPIVTENKKV ENYYLAEEYH QDYLKKNPNG YCHIKFD // ID MNMG_MYCGE Reviewed; 612 AA. AC P47619; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 100. 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=MG379; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 301-394. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71606.1; -; Genomic_DNA. DR EMBL; U01812; AAD12347.1; -; Genomic_DNA. DR PIR; I64241; I64241. DR RefSeq; WP_010869458.1; NC_000908.2. DR ProteinModelPortal; P47619; -. DR EnsemblBacteria; AAC71606; AAC71606; MG_379. DR KEGG; mge:MG_379; -. DR PATRIC; 20010340; VBIMycGen98045_0444. DR KO; K03495; -. DR OMA; FRPGYAI; -. DR OrthoDB; EOG6W9X6J; -. DR BioCyc; MGEN243273:GH2R-434-MONOMER; -. DR Proteomes; UP000000807; 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 1 612 tRNA uridine 5-carboxymethylaminomethyl FT modification enzyme MnmG. FT /FTId=PRO_0000117132. FT NP_BIND 9 14 FAD. {ECO:0000255|HAMAP-Rule:MF_00129}. FT NP_BIND 270 284 NAD. {ECO:0000255|HAMAP-Rule:MF_00129}. SQ SEQUENCE 612 AA; 68995 MW; 67A3F64C985B5912 CRC64; MSFIITVIGA GHAGLEAAFI VSKFNIKVNL LVLDINHLGS CPCNPSIGGP AKGIVTREID VLGGMQAIAA DNNALQYKLL NSSKGPAVQA IRAQIDKIGY KNWFQSQVKL NKNINLIQSE AINLIVRNEK IKGVILKDGS ELLSDAVIIT TGTYLRSKTY CGNTVKNQGP DQSKNSEKLS TNLINRGFKT IRLKTGTPPR ILKTSLDYNQ MELEINNNQN LAFSTTNKNF LPLEKQIPCY LVHTNQKIHD LILKNLKKSA MFNGSISAQG PLYCPSIEDK VFKFSQKPRH QIFVEPESLS LDTIYLAGLS TSFTPEIQKE IIQLLPGFQN AEIKKFGYAI EYDAFLSNQL KPTLETKLIE NLYFAGQING TSGYEEAAGQ GLMAGINAAL KLLKKPPFIL QRNEAYIGVM INDLVTKTIS DPYRLLTSRA EYRLWLRNDN VQERLIKKSF ELGLTDKKTY ELFLKKEKKK QELISFLKNT QVGKVKALKF TNKNTAQSLY DFNKRSEINL DKLIKDLPEK YQLDSETLKQ IEIEIKYEGY IKKNEKYFKG LDKLSKIKIP HTFDYHKVKN LASEAIFKLS NFKPSNLAIA SQIAGVNFND IIAIKHFLKT YE // ID MSRB_MYCGE Reviewed; 150 AA. AC P47686; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000255|HAMAP-Rule:MF_01400}; DE EC=1.8.4.12 {ECO:0000255|HAMAP-Rule:MF_01400}; DE AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01400}; GN Name=msrB {ECO:0000255|HAMAP-Rule:MF_01400}; OrderedLocusNames=MG448; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin. CC {ECO:0000255|HAMAP-Rule:MF_01400}. CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. CC {ECO:0000255|HAMAP-Rule:MF_01400}. CC -!- SIMILARITY: Contains 1 MsrB (methionine-R-sulfoxide reductase) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01126}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC72468.1; -; Genomic_DNA. DR PIR; E64249; E64249. DR RefSeq; WP_009885587.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47686; -. DR SMR; P47686; 4-145. DR STRING; 243273.MgenG_010200000205; -. DR EnsemblBacteria; AAC72468; AAC72468; MG_448. DR KEGG; mge:MG_448; -. DR PATRIC; 20010484; VBIMycGen98045_0515. DR eggNOG; ENOG4105E0X; Bacteria. DR eggNOG; COG0229; LUCA. DR KO; K07305; -. DR OMA; FVHRDDM; -. DR OrthoDB; EOG6091JX; -. DR BioCyc; MGEN243273:GH2R-501-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030091; P:protein repair; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 2.170.150.20; -; 1. DR HAMAP; MF_01400; MsrB; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB. DR InterPro; IPR011057; Mss4-like. DR PANTHER; PTHR10173; PTHR10173; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; SSF51316; 1. DR TIGRFAMs; TIGR00357; TIGR00357; 1. DR PROSITE; PS51790; MSRB; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 150 Peptide methionine sulfoxide reductase FT MsrB. FT /FTId=PRO_0000140283. FT DOMAIN 9 132 MsrB. {ECO:0000255|PROSITE- FT ProRule:PRU01126}. FT ACT_SITE 121 121 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU01126}. SQ SEQUENCE 150 AA; 17290 MW; 62B48D30FF7EFF93 CRC64; MSKYQKKSEA ELKRTLTKLQ FDVTQNAHTE PPYINEYNRN FEKGIYVDIT SGEPLFISTD KFKSGCGWPA FSKPIDKNLI ANYRDESHGM IRTEVRAKNS DSHLGHVFND GPSELGGLRY CINSAALKFI PFEEMEKLGY KDYIHLFKNK // ID MTHFS_MYCGE Reviewed; 165 AA. AC P47487; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase; DE EC=6.3.3.2; DE AltName: Full=5,10-methenyl-tetrahydrofolate synthetase; DE Short=MTHFS; DE Short=Methenyl-THF synthetase; GN OrderedLocusNames=MG245; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Involved in folate metabolism. Catalyzes the CC irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to CC yield 5,10-methenyltetrahydrofolate (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + 5-formyltetrahydrofolate = ADP + CC phosphate + 5,10-methenyltetrahydrofolate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase 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; L43967; AAC71465.1; -; Genomic_DNA. DR PIR; A64227; A64227. DR RefSeq; WP_009885782.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47487; -. DR SMR; P47487; 2-162. DR STRING; 243273.MgenG_010200001677; -. DR EnsemblBacteria; AAC71465; AAC71465; MG_245. DR KEGG; mge:MG_245; -. DR PATRIC; 20009972; VBIMycGen98045_0282. DR eggNOG; ENOG4107XQK; Bacteria. DR eggNOG; COG0212; LUCA. DR KO; K01934; -. DR OrthoDB; EOG6RVG1P; -. DR BioCyc; MGEN243273:GH2R-267-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase 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 Gene3D; 3.40.50.10420; -; 1. DR InterPro; IPR002698; FTHF_cligase. DR InterPro; IPR024185; FTHF_cligase-like. DR PANTHER; PTHR23407:SF1; PTHR23407:SF1; 1. DR Pfam; PF01812; 5-FTHF_cyc-lig; 1. DR PIRSF; PIRSF006806; FTHF_cligase; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 165 5-formyltetrahydrofolate cyclo-ligase. FT /FTId=PRO_0000200287. FT NP_BIND 4 8 ATP. {ECO:0000250}. FT NP_BIND 116 124 ATP. {ECO:0000250}. FT METAL 125 125 Magnesium. {ECO:0000250}. FT METAL 155 155 Magnesium. {ECO:0000250}. FT BINDING 51 51 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 56 56 Substrate. {ECO:0000250}. FT BINDING 126 126 ATP. {ECO:0000250}. FT BINDING 154 154 ATP. {ECO:0000250}. SQ SEQUENCE 165 AA; 19355 MW; AEC4ADEEE55A7020 CRC64; MVDKNSLRKL MLLKRAELND LEKSHLDQKI NQKLMAFLIT RPTIKNLALY IPIKNEVAFL DNFLDFLKLN KITSCFPSIV DQFNMKFIDQ NNNEINPNDI DCFFIPLLAF NKANHRIGFG KGYYDRYLSL TSKKQLKIGI AYDFQYAEFT NDPWDYQLDL IICNG // ID MRAZ_MYCGE Reviewed; 141 AA. AC P47463; Q49315; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 98. DE RecName: Full=Transcriptional regulator MraZ; GN Name=mraZ {ECO:0000255|HAMAP-Rule:MF_01008}; OrderedLocusNames=MG221; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-99. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBUNIT: Forms oligomers. {ECO:0000255|HAMAP-Rule:MF_01008}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP- CC Rule:MF_01008}. CC -!- SIMILARITY: Belongs to the MraZ family. {ECO:0000255|HAMAP- CC Rule:MF_01008}. CC -!- SIMILARITY: Contains 2 SpoVT-AbrB domains. {ECO:0000255|PROSITE- CC ProRule:PRU01076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71442.1; -; Genomic_DNA. DR EMBL; U02195; AAD12481.1; -; Genomic_DNA. DR RefSeq; WP_010869380.1; NC_000908.2. DR ProteinModelPortal; P47463; -. DR SMR; P47463; 1-137. DR STRING; 243273.MgenG_010200001487; -. DR EnsemblBacteria; AAC71442; AAC71442; MG_221. DR KEGG; mge:MG_221; -. DR PATRIC; 20009922; VBIMycGen98045_0257. DR eggNOG; COG2001; LUCA. DR KO; K03925; -. DR OMA; TYECKAD; -. DR OrthoDB; EOG6G4W1C; -. DR BioCyc; MGEN243273:GH2R-243-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell. 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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR HAMAP; MF_01008; MraZ; 1. DR InterPro; IPR003444; MraZ. DR InterPro; IPR020603; MraZ_dom. DR InterPro; IPR007159; SpoVT-AbrB_dom. DR Pfam; PF02381; MraZ; 2. DR ProDom; PD006745; MraZ; 1. DR TIGRFAMs; TIGR00242; TIGR00242; 1. DR PROSITE; PS51740; SPOVT_ABRB; 2. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome; Repeat; KW Transcription; Transcription regulation. FT CHAIN 1 141 Transcriptional regulator MraZ. FT /FTId=PRO_0000108502. FT DOMAIN 5 47 SpoVT-AbrB 1. {ECO:0000255|PROSITE- FT ProRule:PRU01076}. FT DOMAIN 76 119 SpoVT-AbrB 2. {ECO:0000255|PROSITE- FT ProRule:PRU01076}. FT CONFLICT 4 9 GTFNLT -> VPLILP (in Ref. 2; AAD12481). FT {ECO:0000305}. FT CONFLICT 45 45 P -> L (in Ref. 2; AAD12481). FT {ECO:0000305}. SQ SEQUENCE 141 AA; 16307 MW; ADE069FA7C69A936 CRC64; MLLGTFNLTL DNKNRISLPA KLRSFFDSSI VINRGFENCL EIRKPADFES YFQTFNNFPN TQKDTRTLKR LIFANANLVE LDSANRILIP NNLISDAKLD KEIVLIGQFD HLEVWDKVQY EQYLASSESL ETVAERMKDA K // ID NADE_MYCGE Reviewed; 248 AA. AC P47623; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Probable NH(3)-dependent NAD(+) synthetase; DE EC=6.3.1.5; GN Name=nadE; OrderedLocusNames=MG383; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71610.1; -; Genomic_DNA. DR PIR; D64242; D64242. DR RefSeq; WP_009885944.1; NZ_AAGX01000012.1. DR ProteinModelPortal; P47623; -. DR STRING; 243273.MgenG_010200002976; -. DR EnsemblBacteria; AAC71610; AAC71610; MG_383. DR KEGG; mge:MG_383; -. DR PATRIC; 20010350; VBIMycGen98045_0448. DR eggNOG; ENOG4107RW9; Bacteria. DR eggNOG; COG0171; LUCA. DR KO; K01916; -. DR OMA; GLGLPCH; -. DR OrthoDB; EOG64JFM7; -. DR BioCyc; MGEN243273:GH2R-439-MONOMER; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000000807; Chromosome. 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; IEA:UniProtKB-HAMAP. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. 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; 1. DR TIGRFAMs; TIGR00552; nadE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 248 Probable NH(3)-dependent NAD(+) FT synthetase. FT /FTId=PRO_0000152180. FT NP_BIND 30 37 ATP. {ECO:0000250}. FT ACT_SITE 32 32 {ECO:0000250}. SQ SEQUENCE 248 AA; 28190 MW; 45E4BC687545220E CRC64; MTNLIKYLKE LQNWLFDYVK KSKAKGVIFG LSGGIDSAVV AAIAKETFGF ENHLALIMHI NNSKLDFQAT SELVKKMQFN SINIELEESF NLLVKTLGID PKKDFLTAGN IKARLRMITL YAYAQKHNFL VLGTGNFVEY TLGYFTKWGD GACDIAPLAW LLKEDVYKLA KHFNIPEIVI TRAPTASLFE GQTDETEMGI TYKELDQYLK GDLILSSEKQ KIVLDLKAKA EHKHNSPLKF KHLYNFQN // ID NAOX_MYCGE Reviewed; 478 AA. AC Q49408; Q49235; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 92. DE RecName: Full=Probable NADH oxidase; DE Short=NOXase; DE EC=1.6.99.3; GN Name=nox; OrderedLocusNames=MG275; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Catalyzes the four-electron reduction of molecular CC oxygen to water. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. 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 class-III pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD10607.1; 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; L43967; AAC71497.1; -; Genomic_DNA. DR EMBL; U01786; AAD10607.1; ALT_INIT; Genomic_DNA. DR PIR; D64230; D64230. DR ProteinModelPortal; Q49408; -. DR STRING; 243273.MgenG_010200002659; -. DR EnsemblBacteria; AAC71497; AAC71497; MG_275. DR KEGG; mge:MG_275; -. DR PATRIC; 20010050; VBIMycGen98045_0317. DR eggNOG; ENOG4107QMW; Bacteria. DR eggNOG; COG0446; LUCA. DR OrthoDB; EOG6QVRCJ; -. DR BioCyc; MGEN243273:GH2R-304-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0003954; F:NADH dehydrogenase 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 Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR SUPFAM; SSF51905; SSF51905; 1. DR SUPFAM; SSF55424; SSF55424; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; NAD; Oxidation; Oxidoreductase; KW Redox-active center; Reference proteome. FT CHAIN 1 478 Probable NADH oxidase. FT /FTId=PRO_0000184702. FT NP_BIND 8 12 FAD. {ECO:0000250}. FT NP_BIND 111 114 FAD. {ECO:0000250}. FT NP_BIND 170 185 NAD. {ECO:0000250}. FT NP_BIND 295 305 FAD. {ECO:0000250}. FT ACT_SITE 11 11 Proton acceptor. {ECO:0000250}. FT ACT_SITE 43 43 Redox-active. FT BINDING 43 43 FAD. {ECO:0000250}. FT BINDING 197 197 NAD. {ECO:0000250}. FT BINDING 264 264 NAD; via amide nitrogen. {ECO:0000250}. FT BINDING 323 323 FAD; via amide nitrogen. {ECO:0000250}. FT MOD_RES 43 43 Cysteine sulfenic acid (-SOH). FT {ECO:0000250}. FT CONFLICT 28 28 K -> P (in Ref. 2; AAD10607). FT {ECO:0000305}. SQ SEQUENCE 478 AA; 53173 MW; A96A76F64DEBD0C8 CRC64; MKKVIVIGIN HAGTSFIRTL LSKSKDFKVN AYDRNTNISF LGCGIALAVS GVVKNTDDLF YSNPEELKQM GANIFMSHDV TNIDLIKKQV TVRDLTSNKE FTDQFDQLVI ASGAWPICMN VENKVTHKPL EFNYTDKYCG NVKNLISCKL YQHALTLIDS FRKDKTIKSV AIVGSGYIGL ELAEAAWLCK KQVTVIDLLD KPAGNNFDHE FTDELEKVMQ KDGLKLMMGC SVKGFVVDST NNVVKGVETD KGIVNADLVN QSIGFRPSTK FVPKDQNFEF IHNGSIKVNE FLQALNHKDV YVIGGCAAIY NAASEQYENI DLATNAVKSG LVAAMHIIGS NQVKLQSIVG TNALHIFGLN LAACGLTEQR AKKLGFDVGI SVVDDNDRPE FMGSYDKVRF KLVYDKKTLR ILGAQLLSWN TNHSEIIFYI ALAIQKQMLL TELGLVDVYF LPHYNKPFNF VLATVLQALG FSYYIPKK // ID NADK_MYCGE Reviewed; 259 AA. AC P47374; Q49458; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 103. 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 {ECO:0000255|HAMAP-Rule:MF_00361}; OrderedLocusNames=MG128; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 121-180. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Involved in the regulation of the intracellular balance CC of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. CC Catalyzes specifically the phosphorylation on 2'-hydroxyl of the CC adenosine moiety of NAD to yield NADP. {ECO:0000255|HAMAP- CC Rule:MF_00361}. 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 -!- 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; L43967; AAC71346.1; -; Genomic_DNA. DR EMBL; U01806; AAD12334.1; -; Genomic_DNA. DR PIR; B64214; B64214. DR RefSeq; WP_009885682.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47374; -. DR STRING; 243273.MgenG_010200000905; -. DR EnsemblBacteria; AAC71346; AAC71346; MG_128. DR KEGG; mge:MG_128; -. DR PATRIC; 20009660; VBIMycGen98045_0139. DR eggNOG; ENOG4107W91; Bacteria. DR eggNOG; COG0061; LUCA. DR KO; K00858; -. DR OMA; NINNEMH; -. DR OrthoDB; EOG6PZXDR; -. DR BioCyc; MGEN243273:GH2R-132-MONOMER; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; NADP; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 259 NAD kinase. FT /FTId=PRO_0000120637. FT NP_BIND 43 44 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT NP_BIND 111 112 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT ACT_SITE 43 43 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00361}. FT BINDING 136 136 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT CONFLICT 171 180 ELNPLLHPNQ -> RTKPLTYIPT (in Ref. 2; FT AAD12334). {ECO:0000305}. SQ SEQUENCE 259 AA; 29200 MW; 4E225F844F4B3074 CRC64; MKYKIFASTT PQTEPVLNKL RAVLKTWQAV ENGYEYVFVL GGDGFFVSTL ANYNCDSCKV VGINTGHIGF YTSFNGDDLD ENFISKLTSF EFKKINLLEV KTKNHSFLVL NELAVYTNTA YPINIFIDDN HWESYRGSGL LIGPRTGSTA LAKSAKGAVI FPNVDVVQII ELNPLLHPNQ ITIQSPIILP MQTKVEFRIK KAFKAEQFPN FYADGIKLDL KNEDTSISFQ LVLSRSMFHA SLKTKDFIDK LKSTFIKQS // ID NRNA_MYCGE Reviewed; 318 AA. AC P22746; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 09-NOV-2004, sequence version 3. DT 13-APR-2016, entry version 89. DE RecName: Full=Bifunctional oligoribonuclease and PAP phosphatase NrnA; DE EC=3.1.-.-; DE AltName: Full=3'(2'),5'-bisphosphate nucleotidase; DE EC=3.1.3.7; DE AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase; DE Short=PAP phosphatase; DE AltName: Full=Mgp-operon protein 1; DE Short=Mgp1; DE AltName: Full=ORF-1 protein; DE AltName: Full=nanoRNase; GN Name=nrnA; OrderedLocusNames=MG190; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-318. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=2583522; DOI=10.1016/0378-1119(89)90051-6; RA Inamine J.M., Loechel S., Collier A.M., Barile M.F., Hu P.-C.; RT "Nucleotide sequence of the MgPa (mgp) operon of Mycoplasma genitalium RT and comparison to the P1 (mpp) operon of Mycoplasma pneumoniae."; RL Gene 82:259-267(1989). CC -!- FUNCTION: Bifunctional enzyme which has both oligoribonuclease and CC pAp-phosphatase activities. Degrades RNA and DNA oligonucleotides CC with a length of 5 nucleotides and shorter, with a preference for CC longer oligomers. Converts 3'(2')-phosphoadenosine 5'-phosphate CC (PAP) to AMP (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H(2)O = CC adenosine 5'-phosphate + phosphate. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the NrnA oligoribonuclease 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; L43967; AAC71409.1; -; Genomic_DNA. DR EMBL; M31431; AAA25419.1; -; Genomic_DNA. DR PIR; A64221; A64221. DR RefSeq; WP_009886005.1; NZ_AAGX01000020.1. DR ProteinModelPortal; P22746; -. DR STRING; 243273.MgenG_010200003353; -. DR EnsemblBacteria; AAC71409; AAC71409; MG_190. DR KEGG; mge:MG_190; -. DR PATRIC; 20009824; VBIMycGen98045_0218. DR eggNOG; ENOG4107U2Z; Bacteria. DR eggNOG; COG0618; LUCA. DR KO; K06881; -. DR OrthoDB; EOG6FBX0G; -. DR BioCyc; MGEN243273:GH2R-199-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW Complete proteome; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 318 Bifunctional oligoribonuclease and PAP FT phosphatase NrnA. FT /FTId=PRO_0000096465. FT CONFLICT 270 270 D -> E (in Ref. 2; AAC71409/AAA25419). FT {ECO:0000305}. SQ SEQUENCE 318 AA; 36399 MW; F548903DDBE55080 CRC64; MKKGSITEAI NAIKQFDKIV IFHHVRPDGD CLGAQQGLFH LIKANFKNKE VKCVGNNNNL FSFINMTFTN QIDESFLKEA LAIVVDANYK NRIELRELLD KNLFKAVLRI DHHPNEDDLN TSFNFVEESY VACCEQIVEM ATVAKWTIPP VAATLLYIGI YTDSNRFLYS NTSYRTLYLA AILYKAKADI RIVHDHLNHT SLADLKFKKY VYNHFKTQGQ VIYFICTKKI QKRLRMTADQ CARVNLLSNI ADYKIWLFFI EQANNEIRID LRSNGINVRD IAIKYGGGGH NNASGAIITN KKQISDVVSD CVKKIVYN // ID NRDI_MYCGE Reviewed; 153 AA. AC P47472; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Protein NrdI; GN Name=nrdI; OrderedLocusNames=MG230; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Probably involved in ribonucleotide reductase function. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NrdI 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; L43967; AAC71451.1; -; Genomic_DNA. DR PIR; D64225; D64225. DR RefSeq; WP_010869386.1; NC_000908.2. DR ProteinModelPortal; P47472; -. DR STRING; 243273.MgenG_010200001577; -. DR EnsemblBacteria; AAC71451; AAC71451; MG_230. DR KEGG; mge:MG_230; -. DR PATRIC; 20009942; VBIMycGen98045_0267. DR eggNOG; ENOG4105G3E; Bacteria. DR eggNOG; COG1780; LUCA. DR KO; K03647; -. DR OMA; NTHRFVG; -. DR OrthoDB; EOG6W19RD; -. DR BioCyc; MGEN243273:GH2R-252-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 3.40.50.360; -; 1. DR HAMAP; MF_00128; NrdI; 1. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR020852; RNR_Ib_NrdI_bac. DR InterPro; IPR004465; RNR_NrdI. DR Pfam; PF07972; Flavodoxin_NdrI; 1. DR PIRSF; PIRSF005087; NrdI; 1. DR SUPFAM; SSF52218; SSF52218; 1. DR TIGRFAMs; TIGR00333; nrdI; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 153 Protein NrdI. FT /FTId=PRO_0000164321. SQ SEQUENCE 153 AA; 17203 MW; DB94AD5ACD339011 CRC64; MHKDIKLVKE TEIRKPIGSP FIVYFSSISN NTHRFIEKLG FQHKRIPVDI TQSITVSNEY VLICPTYSGG GNQVEGAVPK QVIQFLNNKH NRELCRGVIA SGNTNFGDTF CLAGTVISKK LNVPLLYQFE LLGTKNDVEQ TQKIIANFFQ NSN // ID NUSA_MYCGE Reviewed; 531 AA. AC P47387; Q49227; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000255|HAMAP-Rule:MF_00945}; GN Name=nusA {ECO:0000255|HAMAP-Rule:MF_00945}; OrderedLocusNames=MG141; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-291. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Participates in both transcription termination and CC antitermination. {ECO:0000255|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:0000255|HAMAP- CC Rule:MF_00945}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00945}. CC -!- SIMILARITY: Belongs to the NusA family. {ECO:0000255|HAMAP- CC Rule:MF_00945}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|HAMAP- CC Rule:MF_00945}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|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; L43967; AAC71359.1; -; Genomic_DNA. DR EMBL; U01778; AAD10598.1; -; Genomic_DNA. DR PIR; F64215; F64215. DR RefSeq; WP_009885827.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47387; -. DR STRING; 243273.MgenG_010200002049; -. DR PRIDE; P47387; -. DR EnsemblBacteria; AAC71359; AAC71359; MG_141. DR KEGG; mge:MG_141; -. DR PATRIC; 20009710; VBIMycGen98045_0161. DR eggNOG; ENOG4105CHV; Bacteria. DR eggNOG; COG0195; LUCA. DR KO; K02600; -. DR OMA; PANQIAN; -. DR OrthoDB; EOG6NSGHW; -. DR BioCyc; MGEN243273:GH2R-148-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-HAMAP. 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; IPR004087; KH_dom. 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 SMART; SM00322; KH; 2. 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. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; RNA-binding; KW Transcription; Transcription antitermination; KW Transcription regulation; Transcription termination. FT CHAIN 1 531 Transcription termination/antitermination FT protein NusA. FT /FTId=PRO_0000181971. FT DOMAIN 165 235 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_00945}. FT DOMAIN 340 410 KH. {ECO:0000255|HAMAP-Rule:MF_00945}. FT CONFLICT 278 280 PAV -> ACSW (in Ref. 2; AAD10598). FT {ECO:0000305}. SQ SEQUENCE 531 AA; 59751 MW; 28E61802F55CAF5D CRC64; MKITFISGQE VSLGTSFLLF SKKIVMNELN QPLLAIIKNV AKTKNLSIEE VVFCLKTALE QAYKKHLNFV NVEVNINFDK GIINVEQLFN VVSDENEDYD DFLEIPLQAA NKINSSLQLG DVLRKPIPLK NISSDLINKM IAIFNQKISE TNFKAVMSEF SSEVGEVIEA KVEDIDTNKE GGLKGYIINL ETTKGYISKR ELSKGERLEI GKKYLFVIKE IQRQASLWPI TLSRSDTRLL QFLLTSNTPE IENGTIVIKK IERSPGVKSK IAVISNDPAV DPVAAILGPK GEKIRGISEE FNGEIIDIVF WNEDKLKFLI NAILPAEVIG YNILQDDERD TSIEVVVPAN QIANVFGFKG VNIRLISNLT GWNSVDVYSE KDASEANIKF TRLSFEPEGL FGIKKRREKI ISNDATDKVF YTSKDNVIDD EIIVDLAKDL MVDNKQKQPE QVAKQVVEKS QLEKQVTPKE KEKVQPKAKV HSNSHSKKPA KPNQIFSITV DASDKNLKKD QVDNNQTNPQ TKQTFDSFDD L // ID NUSG_MYCGE Reviewed; 316 AA. AC P47300; Q49344; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Transcription termination/antitermination protein NusG {ECO:0000255|HAMAP-Rule:MF_00948}; GN Name=nusG {ECO:0000255|HAMAP-Rule:MF_00948}; OrderedLocusNames=MG054; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-229 AND 240-316. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Participates in transcription elongation, termination CC and antitermination. {ECO:0000255|HAMAP-Rule:MF_00948}. CC -!- SIMILARITY: Belongs to the NusG family. {ECO:0000255|HAMAP- CC Rule:MF_00948}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71270.1; -; Genomic_DNA. DR EMBL; U01710; AAB01022.1; -; Genomic_DNA. DR EMBL; U02236; AAA03388.1; -; Genomic_DNA. DR PIR; I64205; I64205. DR RefSeq; WP_009885716.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47300; -. DR STRING; 243273.MgenG_010200001145; -. DR EnsemblBacteria; AAC71270; AAC71270; MG_054. DR KEGG; mge:MG_054; -. DR PATRIC; 20009488; VBIMycGen98045_0054. DR eggNOG; ENOG4108545; Bacteria. DR eggNOG; COG0250; LUCA. DR KO; K02601; -. DR OMA; SEDAWRI; -. DR OrthoDB; EOG6FFS95; -. DR BioCyc; MGEN243273:GH2R-54-MONOMER; -. DR Proteomes; UP000000807; Chromosome. 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:0031564; P:transcription antitermination; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.940; -; 1. DR HAMAP; MF_00948; NusG; 1. DR InterPro; IPR006645; NGN_dom. DR InterPro; IPR001062; Transcrpt_antiterm_NusG. DR InterPro; IPR010216; Transcrpt_antiterm_NusG_myco. DR Pfam; PF02357; NusG; 1. DR SMART; SM00738; NGN; 1. DR SUPFAM; SSF82679; SSF82679; 2. DR TIGRFAMs; TIGR01956; NusG_myco; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Transcription; KW Transcription antitermination; Transcription regulation; KW Transcription termination. FT CHAIN 1 316 Transcription termination/antitermination FT protein NusG. FT /FTId=PRO_0000113974. FT CONFLICT 240 241 FL -> LF (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 316 AA; 36323 MW; 852E1D8A7F5E22BB CRC64; MQASELTPKW YVAPVSIKDE AVVKNLKAKI QALGFNHEIV DVKVLKEREV HEEVYSLKSG KLPRSLKNTT FNKWFVLDDY RYLRVKISEK NLLGRYIYIK MIYSEDAWRI VRNFPGITGI VGSSGRGALP IPLDEKDANN LEQMLKGISI NPSKRIMLTN TAIIEMDSDK FDEKFQYILK QKQAIQKPKE DEDSEIVDAE KLKEAFKKLQ NSQEQDEWKE KATIIQSEQT KLDPSVLVPF LGKYEILDTD NKVEQLFEFS VGNLVEVHLT DTIHVQGQIK ALYQGTVNKA VVEIELTSKT QLINLPLENL SFVEFE // ID OBG_MYCGE Reviewed; 433 AA. AC P47624; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 97. 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=MG384; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71611.1; -; Genomic_DNA. DR PIR; E64242; E64242. DR RefSeq; WP_009885945.1; NZ_AAGX01000012.1. DR ProteinModelPortal; P47624; -. DR STRING; 243273.MgenG_010200002981; -. DR EnsemblBacteria; AAC71611; AAC71611; MG_384. DR KEGG; mge:MG_384; -. DR PATRIC; 20010352; VBIMycGen98045_0449. DR eggNOG; ENOG4105C9R; Bacteria. DR eggNOG; COG0536; LUCA. DR KO; K03979; -. DR OMA; TAIYDAD; -. DR OrthoDB; EOG6H1Q1M; -. DR BioCyc; MGEN243273:GH2R-440-MONOMER; -. DR Proteomes; UP000000807; 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; 1. 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 1 433 GTPase Obg. FT /FTId=PRO_0000205441. FT DOMAIN 160 329 OBG-type G. {ECO:0000255|HAMAP- FT Rule:MF_01454}. FT NP_BIND 166 173 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 191 195 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 212 215 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 282 285 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 310 312 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT METAL 173 173 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01454}. FT METAL 193 193 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01454}. SQ SEQUENCE 433 AA; 48166 MW; 08BFC7BC794BC3BE CRC64; MAITDYCECR FTAGNGGNGI IAWKREAHYD KGGPGGGNGG NGGNVILQAD HNCDSLFFLK NKKHLFAEDG QNGKPDLAHG KNGSDLLIKV PIGTTVKNLE NNSVLVDFVH DKQSFILCFG GKGGKGNAAF KSPIMRAPNL YENGDKGEIL NVSLEVKYLA NVGIVGFPNS GKSTLISKLS NAKPKIANYR FTTLIPVLGV VKYQNNSLVF ADIPGLIENA SEGSGLGHDF LRHIERCEIL IHLISLDPVD NDDPCKAYLQ IMDELSKYSP LLVKKKMLVV ANKIDVNEGE KRFKKLEKFL QKKSISVLKI SALKKELGNL LDRVFELYNK TISQFGANKF SLPMELEKHY VFQNTNENNN DPLNIEKDSL NRWIVNCKRL RYWFDKIPQT TLDNIRRLGN KIKEIGIEDQ LKSVGAKKGD IIFFDGCEFV IND // ID OHRL_MYCGE Reviewed; 140 AA. AC P47692; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 2. DT 13-APR-2016, entry version 81. DE RecName: Full=Organic hydroperoxide resistance protein-like; GN OrderedLocusNames=MG454; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the OsmC/Ohr family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC72474.1; 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; L43967; AAC72474.1; ALT_INIT; Genomic_DNA. DR PIR; B64250; B64250. DR RefSeq; WP_041361276.1; NC_000908.2. DR ProteinModelPortal; P47692; -. DR STRING; 243273.MgenG_010200000170; -. DR EnsemblBacteria; AAC72474; AAC72474; MG_454. DR KEGG; mge:MG_454; -. DR PATRIC; 20010498; VBIMycGen98045_0522. DR eggNOG; COG1764; LUCA. DR OMA; ICAYSKA; -. DR OrthoDB; EOG6HQSVF; -. DR BioCyc; MGEN243273:GH2R-507-MONOMER; -. DR Proteomes; UP000000807; 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; IPR019953; OHR. DR InterPro; IPR003718; OsmC/Ohr_fam. DR Pfam; PF02566; OsmC; 1. DR SUPFAM; SSF82784; SSF82784; 1. DR TIGRFAMs; TIGR03561; organ_hyd_perox; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Organic hydroperoxide resistance protein- FT like. FT /FTId=PRO_0000172731. SQ SEQUENCE 140 AA; 15614 MW; 8BB33E4B1939E247 CRC64; MALIYKTVAQ TETGREGSVK TLDGFQTKLS FPKPDLSVQT ENNPEQLFAS AYASCFSQAV IVVMQQHQFS FSKKPVVSVK VELHQENGLF HIKAGVELTT NSNDQEVGKK LIQKAHEMCP FSRLIRNENF LGLTLNGIKL // ID OPPB_MYCGE Reviewed; 407 AA. AC P47323; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Oligopeptide transport system permease protein OppB; GN Name=oppB; OrderedLocusNames=MG077; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for oligopeptides; probably responsible for the translocation of CC the substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. OppBC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71295.1; -; Genomic_DNA. DR PIR; E64208; E64208. DR ProteinModelPortal; P47323; -. DR STRING; 243273.MgenG_010200002886; -. DR EnsemblBacteria; AAC71295; AAC71295; MG_077. DR KEGG; mge:MG_077; -. DR PATRIC; 20009556; VBIMycGen98045_0087. DR eggNOG; ENOG41082QK; Bacteria. DR eggNOG; COG0601; LUCA. DR KO; K15581; -. DR OMA; YHEDAMR; -. DR OrthoDB; EOG6JHRMD; -. DR BioCyc; MGEN243273:GH2R-80-MONOMER; -. DR Proteomes; UP000000807; 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:0015833; P:peptide transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein 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 Cell membrane; Complete proteome; Membrane; Peptide transport; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 407 Oligopeptide transport system permease FT protein OppB. FT /FTId=PRO_0000060139. FT TRANSMEM 9 29 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 101 121 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 134 154 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 179 199 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 238 258 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 288 308 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 97 307 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 407 AA; 45465 MW; F25CBE4C5A4D4E80 CRC64; MFKYILKRLG LAVVAMFIVM SIVFFLVNAT GNVPLSATSA RDIAAVQAQL QEFGFNDPII VRYFRYWAKL FSFQADALGI YYANPNQTIG EIVFARVPNT LYVVLISFLI GSLLGIFLGM VSGLNRGKFL DAAINVLVVL FVSIPSFVVG LGLLKLAGFL NLPPRFINFD DAFFSFDRFL LASIIPILSL VFYSSAAFTY RIRNEVVEVM NQDYIKTAKS KGLGMFAVAR YHIFRNSIIP SIPLFVFGIS GAFSGGFIIE SLFGVQGVSR ILIDSVQVNE TNMVMFNILF IQGIPLLASV FIEFIYVLVD PRIRIANSSN VSLLTKLKFL SSRHQWLMKW NKINSDNAQN IVFNSPLHHQ LLELNAIDYK TKTVQLTTEQ KTALNISATA NFILLGNKCL KLKTIHG // ID OPPC_MYCGE Reviewed; 376 AA. AC P47324; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Oligopeptide transport system permease protein OppC; GN Name=oppC; OrderedLocusNames=MG078; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for oligopeptides; probably responsible for the translocation of CC the substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. OppBC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71296.1; -; Genomic_DNA. DR PIR; F64208; F64208. DR RefSeq; WP_009885933.1; NZ_AAGX01000011.1. DR ProteinModelPortal; P47324; -. DR STRING; 243273.MgenG_010200002891; -. DR EnsemblBacteria; AAC71296; AAC71296; MG_078. DR KEGG; mge:MG_078; -. DR PATRIC; 20009558; VBIMycGen98045_0088. DR eggNOG; ENOG4107RPZ; Bacteria. DR eggNOG; COG1173; LUCA. DR KO; K15582; -. DR OMA; DRIVIDY; -. DR OrthoDB; EOG6HTNTX; -. DR BioCyc; MGEN243273:GH2R-81-MONOMER; -. DR Proteomes; UP000000807; 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:0015833; P:peptide transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. 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; Complete proteome; Membrane; Peptide transport; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 376 Oligopeptide transport system permease FT protein OppC. FT /FTId=PRO_0000060141. FT TRANSMEM 46 66 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 149 169 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 173 193 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 209 229 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 242 262 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 297 317 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 341 361 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 169 366 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 376 AA; 41289 MW; FD6417646F1B09F4 CRC64; MDRNKSFDPN LFKRVDINLL KRNDQLIGKP TTNSIEIIKR LFQNKWAILF FLLIVVIVLL AIIVPLTSPF SAVTPVSTNA LAQNLPPRYL WHKPGDILVH KITARSIAEI SQASGVLVGT LPSANSNPLA TNVQYDIAPF QLQELRNYFP LLGTNGLGID IWTLLWASVA KSLWIAVVVA IIAMVFGTIY GAVAGSFVGH MADNIMSRII EIIDIVPSIL WIIVLGATFR FGGVKQFDDS VVIFTLIFVF WTWPATTTRI YILKNKDTEY IQAAKTLGAH QIRIIFVHML PVVFGRLAVV FVSLIPAVIG YEASLVFLGL KPATDIGLGA LLNQVTSSDN VALILSSIVS FAVLTVAART FANALNDAID PRVVKR // ID ODPA_MYCGE Reviewed; 358 AA. AC P47516; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha; DE EC=1.2.4.1; GN Name=pdhA; OrderedLocusNames=MG274; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2). It contains CC multiple copies of three enzymatic components: pyruvate CC dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and CC lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC -!- SUBUNIT: Heterodimer of an alpha and a beta 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; L43967; AAC71496.1; -; Genomic_DNA. DR PIR; C64230; C64230. DR RefSeq; WP_009885906.1; NZ_AAGX01000009.1. DR ProteinModelPortal; P47516; -. DR STRING; 243273.MgenG_010200002654; -. DR EnsemblBacteria; AAC71496; AAC71496; MG_274. DR KEGG; mge:MG_274; -. DR PATRIC; 20010048; VBIMycGen98045_0316. DR eggNOG; ENOG4107RUY; Bacteria. DR eggNOG; COG1071; LUCA. DR KO; K00161; -. DR OMA; PVDEIEH; -. DR OrthoDB; EOG6VMTKR; -. DR BioCyc; MGEN243273:GH2R-303-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR017596; PdhA/BkdA. DR InterPro; IPR029061; THDP-binding. DR Pfam; PF00676; E1_dh; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR TIGRFAMs; TIGR03181; PDH_E1_alph_x; 1. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; KW Reference proteome; Thiamine pyrophosphate. FT CHAIN 1 358 Pyruvate dehydrogenase E1 component FT subunit alpha. FT /FTId=PRO_0000162200. SQ SEQUENCE 358 AA; 40651 MW; 9C85D2335F80842E CRC64; MAILIKNKVP TTLYQVYDNE GKLIDPNHKI TLTDEQLKHA YYLMNLSRMM DKKMLVWQRA GKMLNFAPNL GEEALQVGMG LGLNENDWVC PTFRSGALML YRGVKPEQLL LYWNGNEKGS QIDAKYKTLP INITIGAQYS HAAGLGYMLH YKKQPNVAVT MIGDGGTAEG EFYEAMNIAS IHKWNTVFCI NNNQFAISTR TKLESAVSDL SVKAIACGIP RVRVDGNDLI ASYEAMQDAA NYARGGNGPV LIEFFSYRQG PHTTSDDPSI YRTKQEEEEG MKSDPVKRLR NFLFDRSILN QAQEEEMFSK IEQEIQAAYE KMVLDTPVSV DEVFDYNYQE LTPELVEQKQ IAKKYFKD // ID OPPD_MYCGE Reviewed; 402 AA. AC P47325; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Oligopeptide transport ATP-binding protein OppD; GN Name=oppD; OrderedLocusNames=MG079; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for oligopeptides. Probably responsible for energy coupling to the CC transport system (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral CC membrane protein {ECO:0000305}. 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; L43967; AAC71297.1; -; Genomic_DNA. DR PIR; G64208; G64208. DR RefSeq; WP_010869322.1; NC_000908.2. DR ProteinModelPortal; P47325; -. DR STRING; 243273.MgenG_010200000595; -. DR EnsemblBacteria; AAC71297; AAC71297; MG_079. DR KEGG; mge:MG_079; -. DR PATRIC; 20009560; VBIMycGen98045_0089. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR KO; K15583; -. DR OMA; SMPSMNT; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-82-MONOMER; -. DR Proteomes; UP000000807; 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:0015833; P:peptide transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein 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; 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; 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; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Peptide transport; Protein transport; KW Reference proteome; Transport. FT CHAIN 1 402 Oligopeptide transport ATP-binding FT protein OppD. FT /FTId=PRO_0000092656. FT DOMAIN 22 309 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 58 65 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 402 AA; 45494 MW; 60DD85496F8DF83F CRC64; MALKRSNFFV DKDQQLKDNL ILDITDLHVN FKVKDGILHA VRGIDLKVER GSIVGIVGES GSGKSVSVKS IIGFNDNAQT KAKLMNFKNV DITKLKKHQW KYYRGTYVSY ISQDPLFSLN PTMTIGKQVK EAIYVASKRR YFQAKSDLKF ALSNKEIDKK TYKSKLKEIK QTYQQKIKPI NVEKKTLEIL QFIGINDAKK RLKAFPSEFS GGMRQRIVIA IAVATEPDLI IADEPTTALD VTIQAKVLTL IKQLRDLLNI TIIFISHNIS LIANFCDFVY VMYAGKIVEQ GLVEEIFTNP LHPYTWALIS SIPEQKDKNK PLTSIPGVIP NMLTPPKGDA FASRNQYALA IDFEYHPPFF EVTKTHKAAT WLLHPQAPKV EPPQAVIDNI TLTKKALQFK DQ // ID ODP2_MYCGE Reviewed; 384 AA. AC P47514; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; DE EC=2.3.1.12; DE AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; DE AltName: Full=E2; GN Name=pdhC; OrderedLocusNames=MG272; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2). It contains CC multiple copies of three enzymatic components: pyruvate CC dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and CC lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine CC = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250}; CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250}; CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral CC symmetry. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 lipoyl-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU01066, 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; L43967; AAC71494.1; -; Genomic_DNA. DR PIR; A64230; A64230. DR RefSeq; WP_009885904.1; NZ_AAGX01000009.1. DR ProteinModelPortal; P47514; -. DR STRING; 243273.MgenG_010200002644; -. DR EnsemblBacteria; AAC71494; AAC71494; MG_272. DR KEGG; mge:MG_272; -. DR PATRIC; 20010044; VBIMycGen98045_0314. DR eggNOG; ENOG4105C7S; Bacteria. DR eggNOG; COG0508; LUCA. DR KO; K00627; -. DR OMA; RIVKVEN; -. DR OrthoDB; EOG610413; -. DR BioCyc; MGEN243273:GH2R-300-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR Gene3D; 3.30.559.10; -; 1. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR023213; CAT-like_dom. DR InterPro; IPR011053; Single_hybrid_motif. DR Pfam; PF00198; 2-oxoacid_dh; 1. DR Pfam; PF00364; Biotin_lipoyl; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00189; LIPOYL; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Glycolysis; Lipoyl; KW Reference proteome; Transferase. FT CHAIN 1 384 Dihydrolipoyllysine-residue FT acetyltransferase component of pyruvate FT dehydrogenase complex. FT /FTId=PRO_0000162281. FT DOMAIN 2 77 Lipoyl-binding. {ECO:0000255|PROSITE- FT ProRule:PRU01066}. FT ACT_SITE 356 356 {ECO:0000255}. FT MOD_RES 43 43 N6-lipoyllysine. {ECO:0000250, FT ECO:0000255|PROSITE-ProRule:PRU01066}. SQ SEQUENCE 384 AA; 41453 MW; BF5585A82425E3A8 CRC64; MANEFKFTDV GEGLHEGKVT EILKQVGDQI KIDEALFVVE TDKVTTELPS PFAGTISAIN VKVGDVVSIG QVMAVIGEKT STPLVEPKPQ PTEEVAKVKE AGASVVGEIK VSDNLFPIFG VKPHATPAVK DTKVASSTNI TVETTQKPES KTEQKTIAIS TMRKAIAEAM TKSHAIIPTT VLTFYVNATK LKQYRESVNG YALSKYSMKI SYFAFFVKAI VNALKKFPVF NASYDPDQNE IVLNDDINVG IAVDTEEGLI VPNIKQAQTK SVVEIAQAIV DLANKARTKK IKLTDLNKGT ISVTNFGSLG AAVGTPIIKY PEMCIVATGN LEERIVKVEN GIAVHTILPL TIAADHRWVD GADVGRFGKE IAKQIEELID LTVA // ID P37_MYCGE Reviewed; 368 AA. AC Q49410; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=High affinity transport system protein p37; DE Flags: Precursor; GN Name=p37; OrderedLocusNames=MG289; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: P37 is part of a high-affinity transport system. CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71510.1; -; Genomic_DNA. DR PIR; I64231; I64231. DR RefSeq; WP_009885873.1; NZ_AAGX01000008.1. DR PDB; 3MYU; X-ray; 1.95 A; A/B=26-368. DR PDBsum; 3MYU; -. DR EnsemblBacteria; AAC71510; AAC71510; MG_289. DR KEGG; mge:MG_289; -. DR PATRIC; 20010106; VBIMycGen98045_0339. DR eggNOG; ENOG4106JMJ; Bacteria. DR eggNOG; ENOG410YA0E; LUCA. DR KO; K02044; -. DR OMA; CARRESN; -. DR OrthoDB; EOG6HB9MH; -. DR BioCyc; MGEN243273:GH2R-324-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR010592; Mycoplasma_p37. DR Pfam; PF06646; Mycoplasma_p37; 1. DR PIRSF; PIRSF004523; Mycoplasma_p37; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal; Transport. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 368 High affinity transport system protein FT p37. FT /FTId=PRO_0000018094. FT LIPID 26 26 N-palmitoyl cysteine. {ECO:0000305}. FT LIPID 26 26 S-diacylglycerol cysteine. {ECO:0000305}. FT STRAND 33 38 {ECO:0000244|PDB:3MYU}. FT HELIX 44 46 {ECO:0000244|PDB:3MYU}. FT HELIX 48 63 {ECO:0000244|PDB:3MYU}. FT STRAND 68 73 {ECO:0000244|PDB:3MYU}. FT HELIX 77 85 {ECO:0000244|PDB:3MYU}. FT STRAND 90 94 {ECO:0000244|PDB:3MYU}. FT HELIX 96 98 {ECO:0000244|PDB:3MYU}. FT STRAND 105 118 {ECO:0000244|PDB:3MYU}. FT HELIX 127 129 {ECO:0000244|PDB:3MYU}. FT HELIX 131 144 {ECO:0000244|PDB:3MYU}. FT HELIX 148 150 {ECO:0000244|PDB:3MYU}. FT TURN 153 157 {ECO:0000244|PDB:3MYU}. FT STRAND 160 163 {ECO:0000244|PDB:3MYU}. FT HELIX 164 166 {ECO:0000244|PDB:3MYU}. FT STRAND 167 185 {ECO:0000244|PDB:3MYU}. FT HELIX 186 198 {ECO:0000244|PDB:3MYU}. FT HELIX 201 205 {ECO:0000244|PDB:3MYU}. FT STRAND 209 211 {ECO:0000244|PDB:3MYU}. FT TURN 217 220 {ECO:0000244|PDB:3MYU}. FT HELIX 221 231 {ECO:0000244|PDB:3MYU}. FT HELIX 238 244 {ECO:0000244|PDB:3MYU}. FT HELIX 246 248 {ECO:0000244|PDB:3MYU}. FT STRAND 249 251 {ECO:0000244|PDB:3MYU}. FT HELIX 254 256 {ECO:0000244|PDB:3MYU}. FT STRAND 265 269 {ECO:0000244|PDB:3MYU}. FT HELIX 272 275 {ECO:0000244|PDB:3MYU}. FT STRAND 294 306 {ECO:0000244|PDB:3MYU}. FT STRAND 309 313 {ECO:0000244|PDB:3MYU}. FT HELIX 318 333 {ECO:0000244|PDB:3MYU}. FT HELIX 340 343 {ECO:0000244|PDB:3MYU}. FT STRAND 347 350 {ECO:0000244|PDB:3MYU}. FT HELIX 354 357 {ECO:0000244|PDB:3MYU}. FT HELIX 359 366 {ECO:0000244|PDB:3MYU}. SQ SEQUENCE 368 AA; 42258 MW; 6286532E78DA96E3 CRC64; MLFKKFTWVI PSLFLTIIST SLLISCATKS DNTLIFNISL DHNADTSIEK FFTVFSKKLS GKLNKKINVN FNIVDDSFTK INNIQANKAD FAFVNSQAIA SNNWFGYTPL IQTLTTAFKE DLELDYYEDG NLQKKAEKTN LLFLSPPYKE WDDIKQKWTG NRYDFLYEPS KLVSFYRSMI LITGSASEIT AIKKAWNEKN WNQFMKFGIG HGQTNSASRF ELPDLLFRKH FAKNYPGLQN AINSDPDKFA VVRGREIGIN KNIKIVFDDA NSFSWTQNIK GSKRPFYTPI DPNDRLEILT YSDPLLYDIG IVSNNLSRIY QKAIGEIFIE LAQSSEDLYG PSIGYNGYKM INDFEKEVVE IIEKTYGK // ID P32_MYCGE Reviewed; 280 AA. AC Q49417; Q49465; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=P32 adhesin; DE AltName: Full=Cytadhesin P32; GN OrderedLocusNames=MG318; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7592348; RA Reddy S.P., Rasmussen W.G., Baseman J.B.; RT "Molecular cloning and characterization of an adherence-related operon RT of Mycoplasma genitalium."; RL J. Bacteriol. 177:5943-5951(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Adhesin necessary for successful cytadherence and CC virulence. CC -!- SUBCELLULAR LOCATION: Cell projection, attachment organelle CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. CC Note=Integral and surface exposed membrane protein that localizes CC to the membrane at the attachment organelle. {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43097; AAA99945.1; -; Genomic_DNA. DR EMBL; L43967; AAC71540.1; -; Genomic_DNA. DR PIR; B64235; B64235. DR RefSeq; WP_010869427.1; NC_000908.2. DR STRING; 243273.MgenG_010200003013; -. DR EnsemblBacteria; AAC71540; AAC71540; MG_318. DR KEGG; mge:MG_318; -. DR PATRIC; 20010166; VBIMycGen98045_0369. DR OMA; PNMQQRP; -. DR OrthoDB; EOG6X3WGQ; -. DR BioCyc; MGEN243273:GH2R-354-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0033111; C:attachment organelle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. 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:0020035; P:cytoadherence to microvasculature, mediated by symbiont protein; IEA:UniProtKB-KW. DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR009896; Cytadhesin_P30. DR Pfam; PF07271; Cytadhesin_P30; 1. PE 3: Inferred from homology; KW Cell membrane; Cell projection; Complete proteome; Cytadherence; KW Membrane; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix; Virulence. FT CHAIN 1 280 P32 adhesin. FT /FTId=PRO_0000058133. FT TRANSMEM 13 37 Helical. {ECO:0000255}. FT TRANSMEM 68 92 Helical. {ECO:0000255}. FT REPEAT 163 168 1-1. FT REPEAT 170 174 2-1. FT REPEAT 186 190 3-1. FT REPEAT 190 195 1-2. FT REPEAT 196 200 2-2. FT REPEAT 199 204 1-3. FT REPEAT 206 210 2-3. FT REPEAT 222 226 3-2. FT REPEAT 226 231 1-4. FT REPEAT 232 236 2-4. FT REPEAT 249 254 1-5. FT REPEAT 256 260 2-5. FT REPEAT 259 264 1-6. FT REGION 163 264 6 X 5 AA repeats of [FM]-N-P-N-M-Q. FT REGION 170 260 5 X 5 AA repeats of R-P-G-F-N. FT REGION 186 226 2 X 5 AA repeats of F-N-P-R-M. FT CONFLICT 18 18 L -> F (in Ref. 1; AAA99945). FT {ECO:0000305}. SQ SEQUENCE 280 AA; 32150 MW; 0BED68C61CE89059 CRC64; MELNGFLRYK KLFIVLALLF TTILIVSLSL LAFALVVKTN GSELGVVFHQ TEDNTTVIQG RSIVEQPWFI PTVAGSFGFS ALAIILGLAI GLPIVKRKEK RLLEEKERQE QIAEQLQRIS DQQEQQTVEI DPQQSQAQPS QPQVQQPLQP QFQQRVPLLR PAFNPNMQQR PGFNQPNQQF QPHNNFNPRM NPNMQRPGFN PNMQQRPGFN QPNQQFQPHN NFNPRMNPNM QRPGFNQPHP NQFAQPNNFN PNMQQRPGFN PNMQQRPNPS QLMPKGGLKP // ID ODPB_MYCGE Reviewed; 326 AA. AC P47515; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta; DE EC=1.2.4.1; GN Name=pdhB; OrderedLocusNames=MG273; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2). It contains CC multiple copies of three enzymatic components: pyruvate CC dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and CC lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71495.1; -; Genomic_DNA. DR PIR; B64230; B64230. DR RefSeq; WP_009885905.1; NZ_AAGX01000009.1. DR ProteinModelPortal; P47515; -. DR STRING; 243273.MgenG_010200002649; -. DR EnsemblBacteria; AAC71495; AAC71495; MG_273. DR KEGG; mge:MG_273; -. DR PATRIC; 20010046; VBIMycGen98045_0315. DR eggNOG; ENOG4105CPP; Bacteria. DR eggNOG; COG0022; LUCA. DR KO; K00162; -. DR OMA; SESYEQM; -. DR OrthoDB; EOG6JQH4C; -. DR BioCyc; MGEN243273:GH2R-302-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 1. 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 PANTHER; PTHR11624; PTHR11624; 1. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR SUPFAM; SSF52922; SSF52922; 1. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; KW Reference proteome; Thiamine pyrophosphate. FT CHAIN 1 326 Pyruvate dehydrogenase E1 component FT subunit beta. FT /FTId=PRO_0000162223. FT BINDING 62 62 Thiamine pyrophosphate. {ECO:0000250}. SQ SEQUENCE 326 AA; 36026 MW; 7C5A0ECCD8A17DD7 CRC64; MSKIQVNNIE ALNNAMDLAL ERDQNVVLYG QDAGFEGGVF RATKGLQQKY GSERVWDCPI AENSMAGIGV GAAIGGLKPI VEIQFSGFSF PAMFQIFVHA ARIRNRSRGV YTAPLVVRMP MGGGIKALEH HSETLEAIYA QIAGLKTVMP SNPYDTKGLF LAAIESPDPV IFFEPKKLYR AFRQEIPSDY YTVPIGEANL ISEGSELTIV SYGPTMFDLI NLVYSGELKD KGIELIDLRT ISPWDKQTVF NSVKKTGRLL VVTEAVKSFT TSAEIITSVT EELFTYLKKA PQRVTGFDIV VPLARGEKYQ FEINARVIDA VNQLLK // ID OPPF_MYCGE Reviewed; 848 AA. AC P47326; Q49263; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Oligopeptide transport ATP-binding protein OppF; GN Name=oppF; OrderedLocusNames=MG080; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 216-317 AND 652-756. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for oligopeptides. Probably responsible for energy coupling to the CC transport system (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral CC membrane protein {ECO:0000305}. 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; L43967; AAC71298.1; -; Genomic_DNA. DR EMBL; U01758; AAD10572.1; -; Genomic_DNA. DR EMBL; U02129; AAD12407.1; -; Genomic_DNA. DR PIR; H64208; H64208. DR RefSeq; WP_009885637.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47326; -. DR STRING; 243273.MgenG_010200000600; -. DR EnsemblBacteria; AAC71298; AAC71298; MG_080. DR KEGG; mge:MG_080; -. DR PATRIC; 20009562; VBIMycGen98045_0090. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG4608; LUCA. DR KO; K10823; -. DR OMA; IMHLGKI; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-83-MONOMER; -. DR Proteomes; UP000000807; 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:0015833; P:peptide transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. 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 SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Peptide transport; Protein transport; KW Reference proteome; Transport. FT CHAIN 1 848 Oligopeptide transport ATP-binding FT protein OppF. FT /FTId=PRO_0000092669. FT DOMAIN 13 785 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 47 54 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT CONFLICT 678 678 A -> S (in Ref. 2; AAD12407). FT {ECO:0000305}. SQ SEQUENCE 848 AA; 98828 MW; 39FD8D6AF316D96C CRC64; MENQNTKKPL VNVKALSMMF KVRGTLFKAL DEIGFTVNEG DFFGVIGESG SGKSTTGKCL IRLNIPSGGK IEIANHLLSG KKLTKENNQW LKQNIQMVFQ DPYSSINPTK NVLTVISEPL VISKTVFGET KQYLKSLQKL SFKVKKTLLR NDIELETKFH NNFFKTVIKQ INESLFNFED LDYKDLKPSH LRQRIINETD KFIEKIRSEF ALFYDFYANQ SVPLQKALDD ANSSLTPSSV IELKNQLKAL QKQAKISKAA WDILQALKQN QKELKDYENY VHFELQKKPR IYLNTWLLTT KSYIKDSKQN MQLTDDIFAF SYNSMVDKKR NLVLILSKYY KLLPYFYDQS VFDNADQFDE IANLIFFDLV ETLLGVTSLF NDALAADKVP LIKFAKFLNK LCDLRFLTLK KSFKKTRVSC SFSFNSEPEI LFANSCYDLQ QMPQIIKPFW EKLFNEQNYQ KIIDSVSRLN VMIANYITKA FEIKKTIDEK LREFKQQNLA LKKAYSANKK SEANKASINE LKVNLKTLKK QLKQEKNTTK KQSKKELKPL LKEHHTALKL HDEFNHDLRK WFKKLNFMVK KYNRLENSQK KFCLVKKLKA LFKKQDETLQ SELRPKLKTF GVINFEYKRA VKESNVFRLV HFAKNIFKPF LFFNLTKIFM RNKVYEALDS VGLKREHAYR YPHEFSGGQR QRIAIARALI TKPKLIIADE LISALDVSIQ AQVINILKDL AKKHNLTVLF IAHDLSMVQT VCNRLIIMHR GKIVERGSVD EIFSNPVHPY TRSLIKASPK LSKINVDLAS FDENFTYDSD YSLTNMPFYI KVPNSEEHEL YCTQKQFDSW IKEATPIN // ID P200_MYCGE Reviewed; 1616 AA. AC Q49429; Q49259; Q49298; Q49352; Q49353; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 76. DE RecName: Full=Protein P200; GN OrderedLocusNames=MG386; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 256-427; 432-543 AND 1083-1140. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Could be an accessory structural component in CC cytadherence. {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71613.1; -; Genomic_DNA. DR EMBL; U02245; AAA03400.1; -; Genomic_DNA. DR EMBL; U02175; AAD12458.1; -; Genomic_DNA. DR EMBL; U02126; AAD12402.1; -; Genomic_DNA. DR PIR; G64242; G64242. DR RefSeq; WP_010869461.1; NC_000908.2. DR ProteinModelPortal; Q49429; -. DR STRING; 243273.MgenG_010200000590; -. DR EnsemblBacteria; AAC71613; AAC71613; MG_386. DR KEGG; mge:MG_386; -. DR PATRIC; 20010358; VBIMycGen98045_0452. DR OMA; QEAKFDS; -. DR OrthoDB; EOG6NGVSD; -. DR BioCyc; MGEN243273:GH2R-443-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0020035; P:cytoadherence to microvasculature, mediated by symbiont protein; IEA:UniProtKB-KW. DR InterPro; IPR022466; AGR_box. DR Pfam; PF16713; EAGR_box; 5. DR TIGRFAMs; TIGR03834; EAGR_box; 4. PE 3: Inferred from homology; KW Complete proteome; Cytadherence; Reference proteome; Repeat. FT CHAIN 1 1616 Protein P200. FT /FTId=PRO_0000058127. FT REPEAT 1161 1186 2-1. FT REPEAT 1205 1236 1-1. FT REPEAT 1310 1339 2-2. FT REPEAT 1358 1389 1-2. FT REGION 891 1389 2 X 26 AA repeats. FT REGION 1205 1389 2 X 32 AA repeats. FT CONFLICT 256 256 P -> S (in Ref. 2; AAA03400). FT {ECO:0000305}. FT CONFLICT 304 304 S -> F (in Ref. 2; AAA03400). FT {ECO:0000305}. SQ SEQUENCE 1616 AA; 185679 MW; 6AF76A13AC49E4FF CRC64; MPKTTKNKNK NTTPKSKTKK YLESANKKSV TKPKKEQDKV ENLFDQPFLG EIKKNILKKT KSFNSKKKET VKSKSKSPID FFDETKRGVF IVPPETDILS RRELNQKTVV NTVPNQTSSY PTINENKLVE LNNQPETKVL ETKKDSFTTT IREKKLNPED SQAFWYIFVG DRKYGFWKNH TWVWLGYFDQ LQRWNYFKVI ETVEVPQEHA AFIKQRPADI DFWRPLVGNP NYGFVQNNTW IWKGFFDKKL NWIPDPVRFT EEALGHTDSL VDEIEKKTIS EQPYWEQEND IVVTVFNTKS LASSLENELL LENSSEEQPV IEEVKPRRNE VIFRNPVTKL HFEKEKFEFL NPVKETNETI PLIEIVKEEV KVESEVEAPV EIEPEAACEP ETTIPEVETV FVYEDDLKGL DSNQTQAGNV PEVETVFVYE DDLKGLDSII KDDQQHDEIA KHVEHLSQDY SKEIKDSAKA DLSNISDDID SVWKEFGSFT DETQKSVEEK SQVDEIILDA NNDFINESLF RDEVVNNIDS QINETVSEQQ FEPTYSVNEF QQEFSEPVVS DEKIKETNSD ESVNTDLTAL FSEKLVNEVL LTNEYVDVNA PFSTETEVKV SSELPKSELV DEITFINNDP KPQEGLEYKV DFLETEPKSL FDEKTTIVVE SEPPFIQPDL SLELDSVNDV DKSLETKTTS VELNHEEIGN EFINLDVSEK EVQEQPTTQL ETDSEFVLPT YQIVEDSFTE SAETPNEFSS EQKDTLEFIS QTQEVETSES NVPTVEQETK LFEHQDENNL FTPLPLDLTE IIESNALFDS KPDEKESSDS ELQPTFKEIK LDSTVEVPQE SSQVEATFDT VQPEAVFDEI KTQELQPEAT TEVVFDDHFQ PDVQPEQTPQ EAKFDSPVEI PQESSQAEFH AEQISDEIKL EEKTEAVFDH QQLENQSEET VVTPTEVTAF EPETIETQLE PSSEDQPSEP ALDQNHPEIV TAEVEQIFDG TKLEDLKLEE ANFDNVENNE VQPKETEAEI TFDETKELQQ ETSSEPLSTE ELKSEATFDN VSEAESEAVF EKPQLETQTE KILEEEPKSE PVDQLITEAS FDTVKHEAVF DKNQTQTEGL EEPQVSSEAE VVDQTTTDTV GEPEAVFDVQ PEKTTEVKFD DVENQQKVIS EPQVEQQPGE AVFEPSAEAK FDSPVESVQD SQPEPVLEEV QTQPEIQPVE SQPEATFDTV QPEQTPQEAK FDSPVETVEQ PEFSSEPTQQ HVESEASFDE PNYDFDEPNY DFDQPSYDSD LQPSEPQYDV DEPNYDFDEP NYEIESKPSE PQFEPQVEQQ PGEAVFEPSA EAKFDSPVES VQDSQPEPLL EEVQTQPEIQ PVESQPEATF DTVQPEQTPQ EAKFDSPVET IQEPQVSSEP EVVVQPNFEE RKPETVLEEP QADEIQPEAS EEESLDWELL VGNNSYGHYE PDGEWVWAGF FGDDQKWNKD ATVKWARERD YLPLIGDEVY GRYNNKGEWI WYGFYDESGD WVLVDEQWKN RQPRINEAPK FWEKLIGNEE YGYYEDNEWN WYDGEFDSEG NWLVFQSEET ENLNEDITKD IPALEGYDID SIDADEWLSQ FSADDAKDVF GSNDKK // ID PARA_MYCGE Reviewed; 269 AA. AC P47706; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 81. DE RecName: Full=ParA family protein MG470; GN OrderedLocusNames=MG470; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the ParA 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; L43967; AAC72491.1; -; Genomic_DNA. DR PIR; I64251; I64251. DR RefSeq; WP_009885563.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47706; -. DR STRING; 243273.MgenG_010200000045; -. DR EnsemblBacteria; AAC72491; AAC72491; MG_470. DR KEGG; mge:MG_470; -. DR PATRIC; 20010538; VBIMycGen98045_0542. DR eggNOG; ENOG4105EZN; Bacteria. DR eggNOG; COG1192; LUCA. DR KO; K03496; -. DR OMA; TFRERNE; -. DR OrthoDB; EOG6D8BCX; -. DR BioCyc; MGEN243273:GH2R-524-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR025669; AAA_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13614; AAA_31; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 269 ParA family protein MG470. FT /FTId=PRO_0000201986. SQ SEQUENCE 269 AA; 29968 MW; 78ADA152C3E67B01 CRC64; MIISFVNNKG GVLKTTMATN VAGSLVKLCP ERRKVILDLD GQGNVSASFG QNPERLNNTL IDILLKVPKF SGSNNFIEID DCLLSVYEGL DILPCNFELN FADIDISRKK YKASDIAEIV KQLAKRYEFV LLDTPPNMAT LVSTAMSLSD VIVIPFEPDQ YSMLGLMRIV ETIDTFKEKN TNLKTILVPT KVNVRTRLHN EVIDLAKTKA KKNNVAFSKN FVSLTSKSSA AVGYEKLPIS LVSSPSKKYL NEYLEITKEI LNLANYNVH // ID PARC_MYCGE Reviewed; 781 AA. AC P47446; Q49377; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000255|HAMAP-Rule:MF_00937}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00937}; DE AltName: Full=Topoisomerase IV subunit A {ECO:0000255|HAMAP-Rule:MF_00937}; GN Name=parC {ECO:0000255|HAMAP-Rule:MF_00937}; OrderedLocusNames=MG204; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-479. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RA Bailey C.C., Younkins R., Huang W.M., Bott K.F.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Topoisomerase IV is essential for chromosome CC segregation. It relaxes supercoiled DNA. Performs the decatenation CC events required during the replication of a circular DNA molecule. CC {ECO:0000255|HAMAP-Rule:MF_00937}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_00937}. CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. CC {ECO:0000255|HAMAP-Rule:MF_00937}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00937}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00937}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit CC family. ParC type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00937}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71422.1; -; Genomic_DNA. DR EMBL; U25549; AAC43991.1; -; Genomic_DNA. DR PIR; E64222; E64222. DR RefSeq; WP_010869372.1; NC_000908.2. DR ProteinModelPortal; P47446; -. DR EnsemblBacteria; AAC71422; AAC71422; MG_204. DR KEGG; mge:MG_204; -. DR PATRIC; 20009862; VBIMycGen98045_0236. DR KO; K02621; -. DR OMA; GRYAKYI; -. DR OrthoDB; EOG661H5V; -. DR BioCyc; MGEN243273:GH2R-213-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.90.199.10; -; 2. DR HAMAP; MF_00937; ParC_type2; 1. DR InterPro; IPR024946; Arg_repress_C-like. 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 InterPro; IPR005741; TopoIV_A_Gpos. DR Pfam; PF03989; DNA_gyraseA_C; 3. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR TIGRFAMs; TIGR01061; parC_Gpos; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; DNA-binding; Isomerase; Membrane; KW Reference proteome; Topoisomerase. FT CHAIN 1 781 DNA topoisomerase 4 subunit A. FT /FTId=PRO_0000145401. FT ACT_SITE 122 122 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00937}. FT SITE 42 42 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00937}. FT SITE 78 78 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00937}. FT SITE 80 80 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00937}. FT SITE 91 91 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00937}. FT SITE 97 97 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00937}. FT SITE 121 121 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00937}. FT CONFLICT 261 261 P -> R (in Ref. 2; AAC43991). FT {ECO:0000305}. SQ SEQUENCE 781 AA; 88513 MW; F14319CEE305B437 CRC64; MDQKNNNLFQ KAIEEVFAVS FSKYAKYIIQ DRALPDLRDG LKPVQRRILY GMFQMGLKPT TPYKKSARAV GEIMGKYHPH GDSSIYDAII RMSQSWKNNW TTVSIHGNNG SVDGDNAAAM RYTETRLSLY GFELLKDIDK KLVSFINNFD DSEKEPTVLP TLLPNLFING ASGIAAGYAT NIAPHNTNEL LDSLCLRIDQ PNCELKQILK IVKGPDFPTG GNVYFEKSLS DIYQAGKGKF IIQAKYEVNK NLNQIEITQI PYETLKANIV KQIEEIIFDN KLSAIESVID SSDRNGIRII IKHKDFLPAE KIMAFLFKHT QLQVNFNLNN TVIANRFPIQ IGLLSYLDHF LKFCHELIIN KAKYELELAS KRLEIILGLI KAISIIDKII KLIRSAVDKS DAREKLIDNF KFTFNQAEAI VSLRLYQLTN TDIFELNQEQ NELEKTVISS EQLIASEKAR NKLLKKQFEG YKKQFHQQRR SQICGFINQK KVEESELIEN KTYGVLITKA GNYHKFESNQ LLKSTTDFKS ESDTIIFAQT IANTDQIFIV TSLGNIINIP VYKLAFNSKN KLASLVSKKP ILLEYETIVF VGTMNSVNQP ILVLTSKLGM VKRIDLTKLN IKPLKATLCI SLRDKDHLVS AFLQQDDKLI CLVSDHNYYT VFHTNEIPLI SSKGMGVKGM KLKLEDQIKF VVAFEANEPL VMICSDGSVI NLKQTELVVV SRMATAKKLP VKKAINYCFS DATNTQLINF QGKNGSKLIT TSELNQMSKT AISQTRFNKL N // ID P29_MYCGE Reviewed; 245 AA. AC P47532; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Probable ABC transporter ATP-binding protein p29; GN Name=p29; OrderedLocusNames=MG290; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Part of a high-affinity 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; L43967; AAC71511.1; -; Genomic_DNA. DR PIR; A64232; A64232. DR RefSeq; WP_010869409.1; NC_000908.2. DR ProteinModelPortal; P47532; -. DR EnsemblBacteria; AAC71511; AAC71511; MG_290. DR KEGG; mge:MG_290; -. DR PATRIC; 20010108; VBIMycGen98045_0340. DR KO; K02041; -. DR OMA; DEIPMTI; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; MGEN243273:GH2R-325-MONOMER; -. DR Proteomes; UP000000807; 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 1 245 Probable ABC transporter ATP-binding FT protein p29. FT /FTId=PRO_0000092678. FT DOMAIN 7 245 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 39 46 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 245 AA; 28006 MW; 01848DA21BD50AC6 CRC64; MENKPILSFE KVSIIYKKAP LLQNISFKVM AKENVCLLGK SGVGKSSLLN SVTNTKIVKS GLVYFDGVAS NKKEYKKLKK QCSYLDQIPN LIDTDYVYEA ILRSAKQKLT WLQKLICFEP KWIKDKILAI LKEVNLNDYV SCIIKDLSAG QKQRVEIAKL FFKSPKLLLV DEPTTGLDPL TASKIMDLIT DFVKREKITL VFVTHDIDLA LKYSTRIIAL KNHALVLDRL TEKLTKEQLY KIYDN // ID P69_MYCGE Reviewed; 543 AA. AC P47533; Q49219; Q49294; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=ABC transport system permease protein p69; GN Name=p69; OrderedLocusNames=MG291; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93 AND 406-530. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Probably part of a high-affinity transport system. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- DOMAIN: Composed of two homologous domains. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD12453.1; 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; L43967; AAC71512.1; -; Genomic_DNA. DR EMBL; U02171; AAD12453.1; ALT_INIT; Genomic_DNA. DR EMBL; U01768; AAD10585.1; -; Genomic_DNA. DR PIR; B64232; B64232. DR RefSeq; WP_010869410.1; NC_000908.2. DR EnsemblBacteria; AAC71512; AAC71512; MG_291. DR KEGG; mge:MG_291; -. DR PATRIC; 20010110; VBIMycGen98045_0341. DR KO; K02042; -. DR OMA; FESNIRW; -. DR OrthoDB; EOG6TR09N; -. DR BioCyc; MGEN243273:GH2R-326-MONOMER; -. DR Proteomes; UP000000807; 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 InterPro; IPR000515; MetI-like. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 543 ABC transport system permease protein FT p69. FT /FTId=PRO_0000060169. FT TRANSMEM 18 38 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 78 98 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 115 135 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 141 161 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 211 231 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 237 257 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 288 308 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 354 374 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 379 399 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 413 433 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 482 502 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 510 530 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 74 256 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT CONFLICT 519 530 YLIAIEIIFLSV -> LSNCNRNNFSFS (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 543 AA; 63076 MW; 86D3787008839987 CRC64; MITKLFFHQV GDNKKRLIWY WKLLIIIAVL AIVIYSWIDN FSSFNQFGLN VFINNITSLF TPNLNHEYTL VRFLAQTAFF VTGGSFLGFI FAILFSYWTA FKIQPFYIAL PIRLITIVLR AFPVLLFGFL FSNLFNKQLA ATLTISWFSF LWNTKYITTF FENSNLKYFF NKKIREGSGF KAFWTTIFLS ENERLWLFFL YSLEANFRWT TLLSIFGIGG IGQLIVDPLS IRVQFDLVLI PLVVLITFLI FIEVVVFLLS SFVFEKNSED LRPILKTTVI EKRKWKRIIF ILFIVVLISL SLANLVTIDY RINDAEFLQD FFNQFFQLKS NLFSSNDPNI NPILMLVKLT TQAISLISLV VIFSILFGFI SCNLFKKRFS ISFKILLLFV RVVPSILLFR LLDPLFLEAK TTIILVLLIN HGSSYGQLMS INFNKANQNI INNYKNHGMT KGFILWNYLL VENKPNLINI TSDAYDSVIR DLILFGSFGG SIIGSRITNF FERAQFDNLG SVTIPLMVYL IAIEIIFLSV RLTRISVFKN YLY // ID P65H_MYCGE Reviewed; 372 AA. AC P47459; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 61. DE RecName: Full=Proline-rich P65 protein homolog; GN OrderedLocusNames=MG217; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71436.1; -; Genomic_DNA. DR PIR; I64223; I64223. DR RefSeq; WP_010869376.1; NC_000908.2. DR EnsemblBacteria; AAC71436; AAC71436; MG_217. DR KEGG; mge:MG_217; -. DR PATRIC; 20009910; VBIMycGen98045_0252. DR OMA; AYQDPNA; -. DR OrthoDB; EOG6DNTDK; -. DR BioCyc; MGEN243273:GH2R-237-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome; Repeat. FT CHAIN 1 372 Proline-rich P65 protein homolog. FT /FTId=PRO_0000058144. FT REPEAT 29 40 1-1. FT REPEAT 41 52 1-2. FT REPEAT 53 60 2-1. FT REPEAT 61 72 1-3. FT REPEAT 73 80 2-2. FT REPEAT 81 92 1-4. FT REPEAT 93 100 2-3. FT REPEAT 101 112 1-5. FT REPEAT 113 119 2-4. FT REPEAT 120 131 1-6. FT REPEAT 132 138 2-5. FT REPEAT 139 150 1-7. FT REPEAT 151 162 1-8. SQ SEQUENCE 372 AA; 44664 MW; 4C29701D213CE19E CRC64; MEKNRSAFQQ NQQASNQPFN QDQNQYYQDP NQQQFNQSGF DPNQQQFNQP GFDPNQQYYQ DPNQQQFNQA GFDQNQQYYQ DPNQQQFNQP GFDPNQQYYQ DPNQQQFNQA GFDQNQYYQD PNQQQFNQSG FDQNQYYQDP NQQQFNQPSF DLNNQQFNQP GFNQSPAFEI TPQEQKAEQE MFGEEPPQVV REIHELPFEK IRSFLQSDFD SYNFRLNSLK SKLDNALYSL DKTIQNTNEN TANLEAIRHN LEQKIQNQSK QLRTNFDTQK LDDKINELEI RMQKLTRNFE SLSELSKHNS YPNYYEKLLP NGGDSMTNVF EKALMMNLLR TTLPPQPQVQ YYPQPYPYIR PYYDEPIYAG FRRRGYRDDF YE // ID PARE_MYCGE Reviewed; 633 AA. AC P47445; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000255|HAMAP-Rule:MF_00939}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00939}; DE AltName: Full=Topoisomerase IV subunit B {ECO:0000255|HAMAP-Rule:MF_00939}; GN Name=parE {ECO:0000255|HAMAP-Rule:MF_00939}; OrderedLocusNames=MG203; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 406-633. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RA Bailey C.C., Younkins R., Huang W.M., Bott K.F.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Topoisomerase IV is essential for chromosome CC segregation. It relaxes supercoiled DNA. Performs the decatenation CC events required during the replication of a circular DNA molecule. CC {ECO:0000255|HAMAP-Rule:MF_00939}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_00939}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00939}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00939}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00939}; 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_00939}; CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. CC {ECO:0000255|HAMAP-Rule:MF_00939}. CC -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type CC 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00939}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00939}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71421.1; -; Genomic_DNA. DR EMBL; U25549; AAC43990.1; -; Genomic_DNA. DR PIR; D64222; D64222. DR RefSeq; WP_010869371.1; NC_000908.2. DR ProteinModelPortal; P47445; -. DR EnsemblBacteria; AAC71421; AAC71421; MG_203. DR KEGG; mge:MG_203; -. DR PATRIC; 20009860; VBIMycGen98045_0235. DR KO; K02622; -. DR OMA; VINTYRA; -. DR OrthoDB; EOG6P334W; -. DR BioCyc; MGEN243273:GH2R-212-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. 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; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; 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_00939; ParE_type2; 1. DR InterPro; IPR002288; DNA_gyrase_B_C. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005740; ParE_type2. 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; TIGR01058; parE_Gpos; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Isomerase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Topoisomerase. FT CHAIN 1 633 DNA topoisomerase 4 subunit B. FT /FTId=PRO_0000145432. FT DOMAIN 419 534 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT NP_BIND 113 119 ATP. {ECO:0000255|HAMAP-Rule:MF_00939}. FT METAL 425 425 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00939}. FT METAL 499 499 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00939}. FT METAL 499 499 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT METAL 501 501 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT BINDING 5 5 ATP. {ECO:0000255|HAMAP-Rule:MF_00939}. FT BINDING 45 45 ATP. {ECO:0000255|HAMAP-Rule:MF_00939}. FT BINDING 72 72 ATP. {ECO:0000255|HAMAP-Rule:MF_00939}. FT BINDING 337 337 ATP. {ECO:0000255|HAMAP-Rule:MF_00939}. FT SITE 450 450 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT SITE 453 453 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT SITE 506 506 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00939}. FT SITE 619 619 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00939}. SQ SEQUENCE 633 AA; 71569 MW; 249B854169A88CB6 CRC64; MKSNYSATNI KILKGLDAVK KRPGMYIGST DSKGLHHMLW EILANSVDEV LAGYATNITV TLDLNNTITV SDDGRGIPYE IHQDSNISTI DTVFTFLHAG GKFDDQSYKL AGGLHGVGAS VVNALSDHLE VTVKRNGQIY QSVYQAGGKI IQKAKKIGDT TSHGTTVSFH ADPKVFKKAQ FDSNIIKSRL KELSFLFAKL KLTFTDQKTN KTTVFFSTSG LVQFLDEINN TVETLGQKTL IKGEKDGIEV EVVFQFNQSD QETILSFANS IKTFEGGSHE NGFCLAISDV INSYCRKYNL LKEKDKNFQL SEIRQGLNAI IKVNLPEKNI AFEGQTKSKL FSKEVKNVVY ELVQQHYFQF LERNNNDAKL IIDKLLNARK IKEQIKQQRE LKKSLSSPQK EKILFGKLAP CQTKKTSEKE LFIVEGDSAG GTAKMGRDRI FQAILPLRGK VLNVEKINNK KEAITNEEIL TLIFCIGTGI LTNFNIKDLK YGKIIIMTDA DNDGAHIQIL LLTFFYRYMQ PLIELGHVYL ALPPLYKLET KDRKTVKYLW SDLELESVKL KLNNFTLQRY KGLGEMNADQ LWDTTMNPTT RKLVQVKLDD LINAEKQINI FMGEKSDLRK HWIEANINFS VEN // ID PBDGT_MYCGE Reviewed; 341 AA. AC Q9ZB73; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=Processive diacylglycerol beta-glycosyltransferase; DE EC=2.4.1.-; DE AltName: Full=Beta-diglycosyldiacylglycerol synthase; DE Short=Beta-DGS; DE Short=DGlyDAG synthase; DE AltName: Full=Beta-monoglycosyldiacylglycerol synthase; DE Short=Beta-MGS; DE Short=MGlyDAG synthase; DE AltName: Full=Glycosyl-beta-1,6-glycosyldiacylglycerol synthase; DE AltName: Full=UDP-galactose:1,2-dioleoylglycerol 3-beta-D-galactosyltransferase; DE AltName: Full=UDP-glucose:1,2-dioleoylglycerol 3-beta-D-glucosyltransferase; GN OrderedLocusNames=MG335.2; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE RP SPECIFICITY, ENZYME REGULATION, AND SUBCELLULAR LOCATION. RX PubMed=21835921; DOI=10.1074/jbc.M110.214148; RA Andres E., Martinez N., Planas A.; RT "Expression and characterization of a Mycoplasma genitalium RT glycosyltransferase in membrane glycolipid biosynthesis: potential RT target against mycoplasma infections."; RL J. Biol. Chem. 286:35367-35379(2011). CC -!- FUNCTION: Processive glycosyltransferase involved in the CC biosynthesis of both the non-bilayer-prone beta- CC monoglycosyldiacylglycerol and the bilayer-forming membrane lipid CC beta-diglycosyldiacylglycerol. These components contribute to CC regulate the properties and stability of the membrane. Catalyzes CC sequentially the transfers of glucosyl or galactosyl residues from CC UDP-Glc or UDP-Gal to diacylglycerol (DAG) acceptor to form the CC corresponding beta-glycosyl-DAG (3-O-(beta-D-glycopyranosyl)-1,2- CC diacyl-sn-glycerol), which then acts as acceptor to give beta- CC diglycosyl-DAG product (3-O-(beta-D-glycopyranosyl-beta-(1->6)-D- CC glycopyranosyl)-1,2-diacyl-sn-glycerol). Dioleoylglycerol (DOG) is CC a preferred sugar acceptor than 3-O-(beta-D-glucopyranosyl)-1,2- CC dioleoyl-sn-glycerol. {ECO:0000269|PubMed:21835921}. CC -!- CATALYTIC ACTIVITY: UDP-glucose + 1,2-diacyl-sn-glycerol = UDP + CC 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol. CC {ECO:0000269|PubMed:21835921}. CC -!- CATALYTIC ACTIVITY: UDP-galactose + 1,2-diacyl-sn-glycerol = UDP + CC 1,2-diacyl-3-O-(beta-D-galactopyranosyl)-sn-glycerol. CC {ECO:0000269|PubMed:21835921}. CC -!- CATALYTIC ACTIVITY: UDP-glucose + 1,2-diacyl-3-O-(beta-D- CC glucopyranosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-(beta-D- CC glucopyranosyl-(1->6)-O-beta-D-glucopyranosyl)-sn-glycerol. CC {ECO:0000269|PubMed:21835921}. CC -!- CATALYTIC ACTIVITY: UDP-galactose + 1,2-diacyl-3-O-(beta-D- CC galactopyranosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-(beta-D- CC galactopyranosyl-(1->6)-O-beta-D-galactopyranosyl)-sn-glycerol. CC {ECO:0000269|PubMed:21835921}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ENZYME REGULATION: Activated by the negatively charged lipid CC dioleoylphosphatidylglycerol (DOPG) and inhibited by N-(n- CC nonyl)deoxygalactonojirimycin (C9J). CC {ECO:0000269|PubMed:21835921}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=50 uM for UDP-Glc (in the presence of beta-glucosyl-DOG as CC sugar acceptor at pH 8 and 35 degrees Celsius) CC {ECO:0000269|PubMed:21835921}; CC KM=87 uM for UDP-Glc (in the presence of DOG as sugar acceptor CC at pH 8 and 35 degrees Celsius) {ECO:0000269|PubMed:21835921}; CC KM=90 uM for beta-glucosyl-DOG (in the presence of UDP-Gal as CC sugar donor at pH 8 and 35 degrees Celsius) CC {ECO:0000269|PubMed:21835921}; CC KM=234 uM for UDP-Gal (in the presence of DOG as sugar acceptor CC at pH 8 and 35 degrees Celsius) {ECO:0000269|PubMed:21835921}; CC KM=270 uM for DOG (in the presence of UDP-Gal as sugar donor at CC pH 8 and 35 degrees Celsius) {ECO:0000269|PubMed:21835921}; CC KM=479 uM for UDP-Gal (in the presence of beta-glucosyl-DOG as CC sugar acceptor at pH 8 and 35 degrees Celsius) CC {ECO:0000269|PubMed:21835921}; CC Note=Kcat is 0.27 sec(-1) for Glc transfer with DOG as sugar CC acceptor. Kcat is 1.10 sec(-1) for Gal transfer with DOG as CC sugar acceptor. Kcat is 0.004 sec(-1) for Glc transfer with CC beta-glucosyl-DOG as sugar acceptor. Kcat is 0.03 sec(-1) for CC Gal transfer with beta-glucosyl-DOG as sugar acceptor.; CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21835921}. CC -!- MISCELLANEOUS: The local lipid environment around the enzyme CC affects both the extent of head group elongation and total amounts CC of glycolipids produced. {ECO:0000305|PubMed:21835921}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 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; L43967; AAC71559.1; -; Genomic_DNA. DR RefSeq; WP_010869439.1; NC_000908.2. DR ProteinModelPortal; Q9ZB73; -. DR STRING; 243273.MgenG_010200003111; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAC71559; AAC71559; MG_517. DR KEGG; mge:MG_517; -. DR PATRIC; 20010230; VBIMycGen98045_0392. DR eggNOG; COG0463; LUCA. DR KO; K19004; -. DR OMA; GITYIAN; -. DR OrthoDB; EOG6WQD5X; -. DR BioCyc; MGEN243273:GH2R-385-MONOMER; -. DR BRENDA; 2.4.1.315; 3528. DR UniPathway; UPA00894; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IDA:UniProtKB. DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0046467; P:membrane lipid biosynthetic process; IDA:UniProtKB. 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 1: Evidence at protein level; KW Carbohydrate metabolism; Cell membrane; Complete proteome; KW Glycerol metabolism; Glycosyltransferase; Lipid biosynthesis; KW Lipid metabolism; Magnesium; Membrane; Reference proteome; KW Transferase. FT CHAIN 1 341 Processive diacylglycerol beta- FT glycosyltransferase. FT /FTId=PRO_0000059245. SQ SEQUENCE 341 AA; 40881 MW; 52D54E8F0A400DBF CRC64; MDKLVSILVP CYKSKPFLKR FFNSLLKQDL NQAKIIFFND NVADETYEVL QKFKKEHNNL AIEVYCDKQN EGIGKVRDKL VNLVTTPYFY FIDPDDCFNN KNVIKEIVES IKKEDFDLGV LKSMVYLCFL KHDFIIKFLP LKGIFQGRVK LINNNNVNKL NYIKNNDQYI WNIVINTDFF RKLNLTFESR LFEDIPIWYP MFFSSQKIVF IDVIGTNYFI RNDSLSTTIS APRYLNLIQC YEKLYVNLSQ NGSLASFIDP NHKIEARFWR RQMFVWFALF SFEYFKKNFS ESKKILEKLF VFLEKNGVYE RVFQTKNQGI YYIWVQRLKY FKHVLESKSD N // ID PEPF_MYCGE Reviewed; 607 AA. AC P47429; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Oligoendopeptidase F homolog; DE EC=3.4.24.-; GN Name=pepF; OrderedLocusNames=MG183; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-111. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the peptidase M3B 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; L43967; AAC71402.1; -; Genomic_DNA. DR EMBL; U02198; AAD12484.1; -; Genomic_DNA. DR PIR; C64220; C64220. DR RefSeq; WP_009885868.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47429; -. DR STRING; 243273.MgenG_010200002319; -. DR MEROPS; M03.007; -. DR PRIDE; P47429; -. DR EnsemblBacteria; AAC71402; AAC71402; MG_183. DR KEGG; mge:MG_183; -. DR PATRIC; 20009798; VBIMycGen98045_0205. DR eggNOG; ENOG4105DPN; Bacteria. DR eggNOG; COG1164; LUCA. DR KO; K08602; -. DR OMA; KEKWDLT; -. DR OrthoDB; EOG6CCH1Q; -. DR BioCyc; MGEN243273:GH2R-192-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR InterPro; IPR013647; OligopepF_N_dom. DR InterPro; IPR001567; Pept_M3A_M3B. DR InterPro; IPR004438; Peptidase_M3B. DR Pfam; PF01432; Peptidase_M3; 1. DR Pfam; PF08439; Peptidase_M3_N; 1. DR TIGRFAMs; TIGR00181; pepF; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Metalloprotease; KW Protease; Reference proteome; Zinc. FT CHAIN 1 607 Oligoendopeptidase F homolog. FT /FTId=PRO_0000078167. FT ACT_SITE 385 385 {ECO:0000255|PROSITE-ProRule:PRU10095}. FT METAL 384 384 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 388 388 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 391 391 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. SQ SEQUENCE 607 AA; 70889 MW; 471DFFF7E3AE4ED7 CRC64; MKNSYKWDLS VLLNNQSLQA NFLKIQTVSE ALIKAYNNGL CFTNKTSFEQ FLAIDDKFTE LENRYTNYLY NKQNENNLDK EVNDAIFAYQ SFKNNHNLAF STLQQELYNH EKLIKDYLTD PKLAVYKRNL MLVFRDKPHQ LSSQTQSLLS QINPCFNQAE RIFNILSTAD LNLQPVVYQN KKYPINSVSD YQSLLENTNR GIRKACYEKW IEIYWTNRNS LSLSLVENYI QLENFAKLKN HPSYIAQTAF NDEIEVGFID FVYQQVAQFA KTFQAFIRLK KQIYKHVLKV NKVEPYDLTL TLFKTKKSYT IEQAKQDALK VLDLLGDNYI KIVKKAFNEN WIDWLADKNK YTGAYSISNV KGLEHFFILM NFDKTKSSLN TLVHELGHSV HSWYASQHQS QNIDPTIFYA EIASIANELL LCYYELQLYK NNHKQLIASL LSQINHFFGA TTRQIMFSQF EKDTLYLIRV NQKPDFKTLI KIYANTAVKY QGFKPEVVAN KLKKTQYQKS LSHIIAIPHF YAGNFYVYKY AIGQVAGILV AKKINSGDKK MKDNYFKFLS SGSSLAPLET IKLLGIDLTS PQPWQEAHNE VKRWLKIVKQ SFKKLQK // ID PGSA_MYCGE Reviewed; 236 AA. AC P47360; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; DE EC=2.7.8.5; DE AltName: Full=Phosphatidylglycerophosphate synthase; DE Short=PGP synthase; GN Name=pgsA; OrderedLocusNames=MG114; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: This protein catalyzes the committed step to the CC synthesis of the acidic phospholipids. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CDP-diacylglycerol + sn-glycerol 3-phosphate = CC CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate. CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol CC biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step CC 1/2. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase CC class-I 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; L43967; AAC71332.1; -; Genomic_DNA. DR PIR; F64212; F64212. DR STRING; 243273.MgenG_010200000825; -. DR EnsemblBacteria; AAC71332; AAC71332; MG_114. DR KEGG; mge:MG_114; -. DR PATRIC; 20009632; VBIMycGen98045_0125. DR eggNOG; ENOG4105BZQ; Bacteria. DR eggNOG; COG0558; LUCA. DR KO; K00995; -. DR OMA; ALAINGY; -. DR OrthoDB; EOG6WMJ3D; -. DR BioCyc; MGEN243273:GH2R-118-MONOMER; -. DR UniPathway; UPA00084; UER00503. DR Proteomes; UP000000807; 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:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. 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 TIGRFAMs; TIGR00560; pgsA; 1. DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 236 CDP-diacylglycerol--glycerol-3-phosphate FT 3-phosphatidyltransferase. FT /FTId=PRO_0000056777. FT TRANSMEM 39 59 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 120 140 Helical. {ECO:0000255}. FT TRANSMEM 163 183 Helical. {ECO:0000255}. FT TRANSMEM 196 216 Helical. {ECO:0000255}. SQ SEQUENCE 236 AA; 26956 MW; C5C4446DFA917B10 CRC64; MDWKTSEMLF PFPVYMAPLT SKFAAYKKKI ANWLTVYRIF IALPTIIFIA LDNQLGVLAN FSVGAISISL QISLLIGGFL FLTAVISDYL DGYLARKWLA VSNFGKLWDP IADKVIINGV LIALAINGYF HFSLLIVFIV RDLVLDGMRI YAYEKKVVIA ANWLGKWKTI MQMVGIVFSC FVWSFKQSEI ASLNSGLFFW LLTQLPYYLA AVFSIWSFIV YNIQIYQQLK AYNSKL // ID PGK_MYCGE Reviewed; 416 AA. AC P47542; Q49338; Q59521; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=Phosphoglycerate kinase; DE EC=2.7.2.3; GN Name=pgk; OrderedLocusNames=MG300; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55; 204-311 AND 314-414. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho- CC D-glyceroyl phosphate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD12464.1; 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; L43967; AAC71522.1; -; Genomic_DNA. DR EMBL; U02226; AAA03379.1; -; Genomic_DNA. DR EMBL; U02234; AAA03386.1; -; Genomic_DNA. DR EMBL; U02178; AAD12464.1; ALT_INIT; Genomic_DNA. DR PIR; B64233; B64233. DR ProteinModelPortal; P47542; -. DR PRIDE; P47542; -. DR EnsemblBacteria; AAC71522; AAC71522; MG_300. DR KEGG; mge:MG_300; -. DR PATRIC; 20010130; VBIMycGen98045_0351. DR KO; K00927; -. DR OMA; AGHPVGK; -. DR OrthoDB; EOG64N9Z0; -. DR BioCyc; MGEN243273:GH2R-336-MONOMER; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000000807; 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-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1260; -; 1. DR Gene3D; 3.40.50.1270; -; 1. DR HAMAP; MF_00145; Phosphoglyc_kinase; 1. DR InterPro; IPR001576; Phosphoglycerate_kinase. DR InterPro; IPR015901; Phosphoglycerate_kinase_C. DR InterPro; IPR015911; Phosphoglycerate_kinase_CS. DR InterPro; IPR015824; Phosphoglycerate_kinase_N. DR PANTHER; PTHR11406; PTHR11406; 1. DR Pfam; PF00162; PGK; 1. DR PIRSF; PIRSF000724; Pgk; 1. DR PRINTS; PR00477; PHGLYCKINASE. DR SUPFAM; SSF53748; SSF53748; 1. DR PROSITE; PS00111; PGLYCERATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 416 Phosphoglycerate kinase. FT /FTId=PRO_0000145965. FT NP_BIND 371 374 ATP. {ECO:0000250}. FT REGION 27 29 Substrate binding. {ECO:0000250}. FT REGION 65 68 Substrate binding. {ECO:0000250}. FT BINDING 42 42 Substrate. {ECO:0000250}. FT BINDING 128 128 Substrate. {ECO:0000250}. FT BINDING 170 170 Substrate. {ECO:0000250}. FT BINDING 221 221 ATP. {ECO:0000250}. FT BINDING 344 344 ATP. {ECO:0000250}. FT CONFLICT 204 206 SPQ -> KPT (in Ref. 2; AAA03379). FT {ECO:0000305}. SQ SEQUENCE 416 AA; 45380 MW; 2A76E2C294BD92E6 CRC64; MLSSNMLNFK TLQAIDFQNK TVVLRSDFNV PMINGVISDS ERILAGLDTI KFLVKKNCKI VLLSHLSRIK SLEDKLNNKK SLKPVAELLQ QLLPTVKVQF SCKNTGAEVK QKVQALAFGE ILLLENTRYC DVNDKGEIVK LESKNDPELA KFWASLGEIF VNDAFGTAHR KHASNAGIAK YVAKSCIGFL MEKELKNLSY LIQSPQKPFV VVLGGAKVSD KLKVVENLLK LADNILIGGG MVNTFLKAKG KATANSLVEK ELIDVAKQIL DKDTHNKIVL AIDQVMGSEF KDQTGITLDV SDKIQEQYQS YMSLDVGSKT IALFESYLKT AKTIFWNGPL GVFEFTNFAK GTSKIGEIIA KNKTAFSVIG GGDSAAAVKQ MQLSDQFSFI STGGGASLAL IGGEELVGIS DIQKNS // ID PKNS_MYCGE Reviewed; 387 AA. AC P47355; Q49450; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-MAY-2016, entry version 100. DE RecName: Full=Putative serine/threonine-protein kinase; DE EC=2.7.11.1; GN OrderedLocusNames=MG109; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-262 AND 286-376. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC71327.1; 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; L43967; AAC71327.1; ALT_INIT; Genomic_DNA. DR EMBL; U01720; AAC43195.1; -; Unassigned_DNA. DR EMBL; U01748; AAD10561.1; -; Genomic_DNA. DR RefSeq; WP_009885667.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47355; -. DR STRING; 243273.MgenG_010200000790; -. DR EnsemblBacteria; AAC71327; AAC71327; MG_109. DR KEGG; mge:MG_109; -. DR PATRIC; 20009622; VBIMycGen98045_0120. DR eggNOG; ENOG4107QPV; Bacteria. DR eggNOG; COG0515; LUCA. DR KO; K08884; -. DR OMA; ENIAFRC; -. DR OrthoDB; EOG62NX1C; -. DR BioCyc; MGEN243273:GH2R-113-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 387 Putative serine/threonine-protein kinase. FT /FTId=PRO_0000171201. FT DOMAIN 15 344 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 164 164 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. SQ SEQUENCE 387 AA; 44626 MW; 346D35DDF2C15610 CRC64; MEAILKIGDI VENKYQIEKL LNRGGMDSYL FLAKNLNLKN YGPVQKKQYG HLVLKVVQKN PKINENNWKK FLDEMVTTTR VHHSNLVKSF DVVNPFLKIV RGNKTIALNQ IVMIAMEYVD GPSLRQLLNR KGYFSVSEVV YYFTKIVKAI DYLHSFKHQI IHRDLKPENI LFTSDLTDIK LLDFGIASTV VKVAEKTEVL TDENSLFGTV SYMIPDVLES TVNKAGKKVR KPPNAQYDIY SLGIILFEML VGRVPFNKSI NPNKERETIQ KARNFDLPLM QATRSDIPNS LENIAFRCTA VKRENNKWLY SSTKELLEDL ANWENEQAMI KPANERVLEG QVEIREMMLE KPLAWYFKTW ALSIFTIVFI GLIIAAIVLL LIFNARF // ID PFKA_MYCGE Reviewed; 323 AA. AC P47457; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 104. DE RecName: Full=Probable ATP-dependent 6-phosphofructokinase; DE Short=ATP-PFK; DE Short=Phosphofructokinase; DE EC=2.7.1.11; DE AltName: Full=Phosphohexokinase; GN Name=pfkA; Synonyms=pfk; OrderedLocusNames=MG215; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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:0000250|UniProtKB:P0A796}. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. {ECO:0000250|UniProtKB:P0A796}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P0A796}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000250|UniProtKB:P0A796}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A796}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A796}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) 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; L43967; AAC71434.1; -; Genomic_DNA. DR PIR; G64223; G64223. DR RefSeq; WP_010869375.1; NC_000908.2. DR ProteinModelPortal; P47457; -. DR EnsemblBacteria; AAC71434; AAC71434; MG_215. DR KEGG; mge:MG_215; -. DR PATRIC; 20009890; VBIMycGen98045_0250. DR KO; K00850; -. DR OMA; MNATIAY; -. DR OrthoDB; EOG644ZRM; -. DR BioCyc; MGEN243273:GH2R-227-MONOMER; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-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:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. 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. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 323 Probable ATP-dependent 6- FT phosphofructokinase. FT /FTId=PRO_0000111963. FT NP_BIND 72 73 ATP. {ECO:0000250|UniProtKB:P0A796}. FT NP_BIND 102 105 ATP. {ECO:0000250|UniProtKB:P0A796}. FT REGION 125 127 Substrate binding. FT {ECO:0000250|UniProtKB:P0A796}. FT REGION 169 171 Substrate binding. FT {ECO:0000250|UniProtKB:P0A796}. FT REGION 253 256 Substrate binding. FT {ECO:0000250|UniProtKB:P0A796}. FT ACT_SITE 127 127 Proton acceptor. FT {ECO:0000250|UniProtKB:P0A796}. FT METAL 103 103 Magnesium; catalytic. FT {ECO:0000250|UniProtKB:P0A796}. FT BINDING 11 11 ATP; via amide nitrogen. FT {ECO:0000250|UniProtKB:P0A796}. FT BINDING 162 162 Substrate; shared with dimeric partner. FT {ECO:0000250|UniProtKB:P0A796}. FT BINDING 221 221 Substrate. FT {ECO:0000250|UniProtKB:P0A796}. SQ SEQUENCE 323 AA; 35641 MW; 67072AC3D5542E89 CRC64; MDKIAILTSG GDASGMNATI AYLTKYAIAK QLEVFYVKNG YYGLYHNHFI TSKELDLTDF FFMGGTVIGS SRFKQFQDPS LRKQAVLNLK KRGINNLVVI GGDGSYMGAK ALSELGLNCF CLPGTIDNDV NSSEFTIGFW TALEAIRVNV EAIYHTTKSH NRLAIIEVMG RDCSDLTIFG GLATNASFVV TSKNSLDLNG FEKAVRKVLQ FQNYCVVLVS ENIYGKNGLP SLEMVKEHFE NNAIKCNLVS LGHTQRGFSP NSIELFQISL MAKHTIDLVV NNANSQVIGM KNNQAVNYDF NTAFNLPKAD RTKLLNQVNT AII // ID PLSC_MYCGE Reviewed; 268 AA. AC Q49402; Q49287; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase; DE Short=1-AGP acyltransferase; DE Short=1-AGPAT; DE EC=2.3.1.51; DE AltName: Full=Lysophosphatidic acid acyltransferase; DE Short=LPAAT; GN Name=plsC; OrderedLocusNames=MG212; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-105. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic CC acid by incorporating acyl moiety at the 2 position. CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CC CoA + 1,2-diacyl-sn-glycerol 3-phosphate. CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3. 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:0000250}. CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate CC acyltransferase 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; L43967; AAC71431.1; -; Genomic_DNA. DR EMBL; U02160; AAD12442.1; -; Genomic_DNA. DR PIR; D64223; D64223. DR RefSeq; WP_009885752.1; NZ_AAGX01000004.1. DR ProteinModelPortal; Q49402; -. DR STRING; 243273.MgenG_010200001427; -. DR EnsemblBacteria; AAC71431; AAC71431; MG_212. DR KEGG; mge:MG_212; -. DR PATRIC; 20009884; VBIMycGen98045_0247. DR eggNOG; ENOG4107RIS; Bacteria. DR eggNOG; COG0204; LUCA. DR KO; K00655; -. DR OMA; KVAYNAF; -. DR OrthoDB; EOG6ZWJDH; -. DR BioCyc; MGEN243273:GH2R-224-MONOMER; -. DR UniPathway; UPA00557; UER00613. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. 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; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1 268 Probable 1-acyl-sn-glycerol-3-phosphate FT acyltransferase. FT /FTId=PRO_0000208172. FT MOTIF 92 97 HXXXXD motif. FT CONFLICT 2 2 Missing (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 268 AA; 30469 MW; A88B07D2BC4C6A4A CRC64; MDKLFKTSFR FIIRFLQILS LPVVFPYFLL SFLACLITSK NYESLPYNYP PEIRFKKVYR LVSMWLYIKG IKVVTVNDKI IPKKPVLVVA NHKSNLDPLV LIKAFGRLKN SPPLTFVAKI ELKDTVLFKL MKLIDCVFID RKNIRQIANA LETQQQLIRQ GTAIAVFAEG TRILSNDIGE FKPGALKVAY NAFVPILPVS IVGSLGKMES NKRLKEHGVK KSSNYEVKVI FNKLINPISF NQIDSNNLAN NIRSIISDAY TSEKPSND // ID PIP_MYCGE Reviewed; 308 AA. AC P47266; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=Putative proline iminopeptidase; DE Short=PIP; DE EC=3.4.11.5; DE AltName: Full=Prolyl aminopeptidase; DE Short=PAP; GN Name=pip; OrderedLocusNames=MG020; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-308. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Specifically catalyzes the removal of N-terminal proline CC residues from peptides. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal proline from a peptide. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S33 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; L43967; AAC71236.1; -; Genomic_DNA. DR EMBL; U02229; AAA03381.1; -; Genomic_DNA. DR PIR; B64202; B64202. DR RefSeq; WP_009885920.1; NZ_AAGX01000010.1. DR ProteinModelPortal; P47266; -. DR STRING; 243273.MgenG_010200002781; -. DR ESTHER; mycge-pip; Proline_iminopeptidase. DR MEROPS; S33.001; -. DR EnsemblBacteria; AAC71236; AAC71236; MG_020. DR KEGG; mge:MG_020; -. DR PATRIC; 20009416; VBIMycGen98045_0018. DR eggNOG; ENOG4107RCM; Bacteria. DR eggNOG; COG0596; LUCA. DR KO; K01259; -. DR OMA; YDPGIRD; -. DR OrthoDB; EOG6BPDDC; -. DR BioCyc; MGEN243273:GH2R-20-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR002410; Peptidase_S33. DR InterPro; IPR005944; Pro_iminopeptidase. DR Pfam; PF00561; Abhydrolase_1; 1. DR PIRSF; PIRSF006431; Pept_S33; 1. DR PRINTS; PR00793; PROAMNOPTASE. DR SUPFAM; SSF53474; SSF53474; 1. DR TIGRFAMs; TIGR01249; pro_imino_pep_1; 1. PE 3: Inferred from homology; KW Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Protease; KW Reference proteome. FT CHAIN 1 308 Putative proline iminopeptidase. FT /FTId=PRO_0000080839. FT ACT_SITE 105 105 Nucleophile. {ECO:0000250}. FT ACT_SITE 261 261 {ECO:0000250}. FT ACT_SITE 289 289 Proton donor. {ECO:0000250}. SQ SEQUENCE 308 AA; 35289 MW; 65087048D205EEF3 CRC64; MNTKLNVKGY LNVGDNHQLY YWTQGNPNGK PVLYIHGGPG SGTDEGCLKY FDLETTWIIL LDQRGCGKSK TNDIFYENNT DKLVSDFEIL RQKLNIKNWT LFGGSWGSAL ALVYAIKHPQ VVDKIFLRAL FLAREKDWSE ALMGLGKMFY PYEHQRFMDS IPKAYQNSYE QIVNYCYDQF QNGDESTKEK LAKAWVDWES TLLSPINKIH STATDFKLVE KLALLECHYA VNKSFLDENF ILDNISVLKN KSIYLAHGRF DLICPLYQPL ALKQAFPELQ LYVTNNAGHS GSDANNLATI KHLLKTYL // ID PLSY_MYCGE Reviewed; 239 AA. AC P47489; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Acyl-PO4 G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043}; DE Short=GPAT {ECO:0000255|HAMAP-Rule:MF_01043}; DE EC=2.3.1.n3 {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Lysophosphatidic acid synthase {ECO:0000255|HAMAP-Rule:MF_01043}; DE Short=LPA synthase {ECO:0000255|HAMAP-Rule:MF_01043}; GN Name=plsY {ECO:0000255|HAMAP-Rule:MF_01043}; OrderedLocusNames=MG247; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 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; L43967; AAC71467.1; -; Genomic_DNA. DR PIR; C64227; C64227. DR RefSeq; WP_009885785.1; NZ_AAGX01000005.1. DR STRING; 243273.MgenG_010200001692; -. DR EnsemblBacteria; AAC71467; AAC71467; MG_247. DR KEGG; mge:MG_247; -. DR PATRIC; 20009976; VBIMycGen98045_0284. DR eggNOG; ENOG4107Y8I; Bacteria. DR eggNOG; COG0344; LUCA. DR KO; K08591; -. DR OMA; HSQYPKI; -. DR OrthoDB; EOG6M6JSX; -. DR BioCyc; MGEN243273:GH2R-269-MONOMER; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000000807; 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 membrane; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 239 Glycerol-3-phosphate acyltransferase. FT /FTId=PRO_0000188402. FT TRANSMEM 6 26 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 61 81 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 99 119 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 135 155 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 159 179 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 199 219 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. SQ SEQUENCE 239 AA; 27489 MW; D78CE976DEF621FD CRC64; MNQASAIAIL VIFSLASGYL LGSIIFADIF SKILKKNVRE FGSKNPGATN SMRVFGLKIG FLVAIFDAFK GFFAFLLTWI LFRFGLQGYL TEKVYQSTYF LSYLSCFAAT IGHIFPLYFK FKGGKAIATT GGSLLAISLW WFLICLLIWI MITLITKYVS LASLITFFVL AVIILIPWLD YLYFFNSDPL KSITYQNEWY IILFFCLWYW PLTVVVFWLH RANIIRILHG KESKITQLN // ID POTA_MYCGE Reviewed; 559 AA. AC P47288; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 112. 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}; OrderedLocusNames=MG042; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 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; L43967; AAC71258.1; -; Genomic_DNA. DR RefSeq; WP_010869303.1; NC_000908.2. DR ProteinModelPortal; P47288; -. DR SMR; P47288; 30-65. DR EnsemblBacteria; AAC71258; AAC71258; MG_042. DR KEGG; mge:MG_042; -. DR PATRIC; 20009462; VBIMycGen98045_0041. DR KO; K11072; -. DR OMA; RQKMQVL; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-42-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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; -; 2. 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 Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 2. 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 membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 559 Spermidine/putrescine import ATP-binding FT protein PotA. FT /FTId=PRO_0000092750. FT DOMAIN 7 448 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01726}. FT NP_BIND 40 47 ATP. {ECO:0000255|HAMAP-Rule:MF_01726}. FT REGION 108 317 Insert. SQ SEQUENCE 559 AA; 65192 MW; DB8F04B26A110F6F CRC64; MNEHSLIEIE GLNKTFDDGY VSIRDISLNI KKGEFITILG PSGCGKTTLL RLLAGFEDPT YGKIKVNGID IKDMAIHKRP FATVFQDYAL FSHLTVYKNI AYGLKVMWTK LDEIPKLVSD YQKQLALKHL KLERKIEQLQ KNNSNAQRIK KLKEKLQKLL EINKQKVIEF ENKEKLRRED IYKNLEQLTK EWDLLSQKKL KEVEQQKQAI DKSFEKVENK YKKDPWFFQH SEIRLKQYQK KKTELKADIK ATKNKEQIQK LTKELQTLKQ KYANKKAIDK EYDKLVVAYN KKDYWTSYWE TYTLQQKEAF EKRYLSRKLT KAEQNKKVSD VIEMVGLKGK EDRLPDELSG GMKQRVALAR SLVVEPEILL LDEPLSALDA KVRKNLQKEL QQIHKKSGLT FILVTHDQEE ALVLSDRIVV MNEGNILQVG NPVDIYDSPK TEWIANFIGQ ANIFKGTYLG EKKIQLQSGE IIQTDVDNNY VVGKQYKILI RPEDFDLVPE NKGFFNVRVI DKNYKGLLWK ITTQLKDNTI VDLESVNEVD VNKTFGVLFD PIDVHLMEV // ID POTC_MYCGE Reviewed; 284 AA. AC P47290; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Spermidine/putrescine transport system permease protein PotC homolog; GN Name=potC; OrderedLocusNames=MG044; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Required for the activity of the bacterial transport CC system of putrescine and spermidine. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. CysTW subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71260.1; -; Genomic_DNA. DR PIR; H64204; H64204. DR RefSeq; WP_009885706.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47290; -. DR STRING; 243273.MgenG_010200001085; -. DR EnsemblBacteria; AAC71260; AAC71260; MG_044. DR KEGG; mge:MG_044; -. DR PATRIC; 20009466; VBIMycGen98045_0043. DR eggNOG; ENOG4105D38; Bacteria. DR eggNOG; COG1177; LUCA. DR KO; K11070; -. DR OMA; TERINYK; -. DR OrthoDB; EOG6HMXBZ; -. DR BioCyc; MGEN243273:GH2R-44-MONOMER; -. DR Proteomes; UP000000807; 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 Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 284 Spermidine/putrescine transport system FT permease protein PotC homolog. FT /FTId=PRO_0000060185. FT TRANSMEM 13 33 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 76 96 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 116 136 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 143 163 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 189 209 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 242 262 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 72 263 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 284 AA; 31669 MW; 2746C49F2C3AF175 CRC64; MKKHFKNLIK NSYFFLLITL IYLPLLIVVL VSLNGSSSRG NIVLDFGNVL NPNPDSKSAY LRLGETDFAT PLINSIIIGV ITVLVSVPIA VISAFALLRT RNALKKTIFG ITNFSLATPD IITAISLVLL FANTWLSFNQ QLGFFTIITS HISFSVPYAL ILIYPKIQKL NPNLILASQD LGYSPLKTFF HITLPYLMPS IFSAVLVVFA TSFDDYVITS LVQGSVKTIA TELYSFRKGI KAWAIAFGSI LILISVLGVC LITLQKYLRE KRKEIIKIRQ WKNS // ID PLSX_MYCGE Reviewed; 328 AA. AC Q49427; Q49240; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 92. 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}; OrderedLocusNames=MG368; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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=AAD10614.1; 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; L43967; AAC71595.1; -; Genomic_DNA. DR EMBL; U01791; AAD10614.1; ALT_INIT; Genomic_DNA. DR PIR; G64240; G64240. DR RefSeq; WP_009885824.1; NZ_AAGX01000006.1. DR ProteinModelPortal; Q49427; -. DR STRING; 243273.MgenG_010200002013; -. DR EnsemblBacteria; AAC71595; AAC71595; MG_368. DR KEGG; mge:MG_368; -. DR PATRIC; 20010318; VBIMycGen98045_0433. DR eggNOG; ENOG4105C6B; Bacteria. DR eggNOG; COG0416; LUCA. DR KO; K03621; -. DR OMA; VPSDVKN; -. DR OrthoDB; EOG68H88P; -. DR BioCyc; MGEN243273:GH2R-423-MONOMER; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000000807; 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 1 328 Phosphate acyltransferase. FT /FTId=PRO_0000189905. SQ SEQUENCE 328 AA; 36502 MW; 7783F31DDC1D4A3F CRC64; MAFRFAVDCL GFENKPSEAI EAVLKYWSFH QDLNFILIGD EKAFDGLDIL PKNITKKLAN SFIEMTDTPL SARRKVNSSM QIAINLVREG NADVVISAGS SAVYASLTND AFGKINKNTK SAFMSYVPTD NNNWFYFLDV GANKYFTGKE LYFLGLMADI FVKKTTTKKT PKIGLLNIGT EENKGFDYHQ EAFKLLKADK NLNFLGFVES RFLLDGICDI LIADGYSGNL VLKAMEGTFK TIARILKRGY KRNPLAGLFS LGIIKSVAKK FDYKNNAGAV VMGLNKLALK THGSADKQQF LSTIRLAHLS LKSDLINAIK TSLNNYEE // ID PPH_MYCGE Reviewed; 260 AA. AC P47354; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Putative protein phosphatase; DE EC=3.1.3.16; GN OrderedLocusNames=MG108; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-260. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O CC = [a protein]-serine/threonine + phosphate. CC -!- SIMILARITY: Contains 1 PPM-type phosphatase domain. CC {ECO:0000255|PROSITE-ProRule:PRU01082}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71326.1; -; Genomic_DNA. DR EMBL; U02111; AAD12384.1; -; Genomic_DNA. DR PIR; I64211; I64211. DR RefSeq; WP_010869334.1; NC_000908.2. DR ProteinModelPortal; P47354; -. DR STRING; 243273.MgenG_010200000785; -. DR EnsemblBacteria; AAC71326; AAC71326; MG_108. DR KEGG; mge:MG_108; -. DR PATRIC; 20009620; VBIMycGen98045_0119. DR eggNOG; ENOG41080P2; Bacteria. DR eggNOG; COG0631; LUCA. DR KO; K01090; -. DR OMA; VREENQD; -. DR OrthoDB; EOG65N17S; -. DR BioCyc; MGEN243273:GH2R-112-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro. DR Gene3D; 3.60.40.10; -; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR001932; PPM-type_phosphatase_dom. DR PANTHER; PTHR13832; PTHR13832; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; SSF81606; 1. DR PROSITE; PS51746; PPM_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Protein phosphatase; Reference proteome. FT CHAIN 1 260 Putative protein phosphatase. FT /FTId=PRO_0000057795. FT DOMAIN 9 254 PPM-type phosphatase. FT {ECO:0000255|PROSITE-ProRule:PRU01082}. SQ SEQUENCE 260 AA; 29960 MW; 5C6BBC107F2539B9 CRC64; MQAANDHFFT GLSKKGPVRK ENQDFYGFSF NQNNLLIVVC DGLGGYKGGK IASNLVGKLF LSLFEGFEFN QWDETTVKKW FENTLIQARF QLENCFQTVY EAQIQFARMA STLVLGILTK SDIYIFWIGD SRAYLLFENQ AKLVTKDHNL YNQLVAMNAD EKLLLSYSNQ LLALTNTISK ETKRPLVYGF YNTKIEQQEF LLLCSDGLYN FVEKELFFEI ITNSKNLKQA VFNLYRKSIE NASNDNITAA LVNLQKWKQS // ID POTB_MYCGE Reviewed; 285 AA. AC P47289; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Spermidine/putrescine transport system permease protein PotB homolog; GN Name=potB; OrderedLocusNames=MG043; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Required for the activity of the bacterial transport CC system of putrescine and spermidine. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. CysTW subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71259.1; -; Genomic_DNA. DR PIR; G64204; G64204. DR RefSeq; WP_010869304.1; NC_000908.2. DR ProteinModelPortal; P47289; -. DR EnsemblBacteria; AAC71259; AAC71259; MG_043. DR KEGG; mge:MG_043; -. DR PATRIC; 20009464; VBIMycGen98045_0042. DR KO; K11071; -. DR OMA; QNSEFIN; -. DR OrthoDB; EOG6HMXBZ; -. DR BioCyc; MGEN243273:GH2R-43-MONOMER; -. DR Proteomes; UP000000807; 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 Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 285 Spermidine/putrescine transport system FT permease protein PotB homolog. FT /FTId=PRO_0000060179. FT TRANSMEM 10 30 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 62 82 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 94 114 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 136 156 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 196 216 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 247 267 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 58 268 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 285 AA; 32101 MW; DED3041909865D6B CRC64; MHIKKKYWLL LPFFLLMTIF FIIPMAWIIV SGLQSEDGAS ISQKYEPLVS GLGFFNSFWT SLWISIVTVI VALLFSFPFC YFLSQSKNKI FKAFVISIAT VPIWSSFLIK LIGLKTLLDL LIGLSLNRVG DNNLTFGSGY TLLGTIYLFT PFMFLPLYNH FCVLPKNLLL ASQDLGYNWI YSFVKVVIPF SKTAMLSGIA LTFFPALTSV AIAQFLDNSN QAETLGNYIF TLGNNGYDSA IERGRAAGAI IIAALITFAI YFTVVFLPKI VRIVHNKWKQ HEKAF // ID PSTA_MYCGE Reviewed; 654 AA. AC P47651; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=Phosphate transport system permease protein PstA homolog; GN Name=pstA; OrderedLocusNames=MG411; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 136-211. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Could be part of a binding-protein-dependent transport CC system for phosphate; probably responsible for the translocation CC of the substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. CysTW subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 ABC transmembrane type-1 domains. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71639.1; -; Genomic_DNA. DR EMBL; U01746; AAD10559.1; -; Genomic_DNA. DR PIR; E64245; E64245. DR RefSeq; WP_010869471.1; NC_000908.2. DR ProteinModelPortal; P47651; -. DR EnsemblBacteria; AAC71639; AAC71639; MG_411. DR KEGG; mge:MG_411; -. DR PATRIC; 20010414; VBIMycGen98045_0480. DR KO; K02037; -. DR KO; K02038; -. DR OMA; PYHLFIL; -. DR OrthoDB; EOG6HMXBZ; -. DR BioCyc; MGEN243273:GH2R-468-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:InterPro. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR005672; Phosphate_PstA. DR Pfam; PF00528; BPD_transp_1; 2. DR SUPFAM; SSF161098; SSF161098; 2. DR TIGRFAMs; TIGR00974; 3a0107s02c; 1. DR PROSITE; PS50928; ABC_TM1; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Phosphate transport; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 654 Phosphate transport system permease FT protein PstA homolog. FT /FTId=PRO_0000060204. FT TRANSMEM 22 42 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 64 84 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 113 133 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 143 163 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 266 286 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 303 323 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 368 388 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 417 437 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 453 473 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 486 506 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 535 555 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 613 633 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 70 285 ABC transmembrane type-1 1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 413 623 ABC transmembrane type-1 2. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 654 AA; 73526 MW; 997BD093F7A907B4 CRC64; MQKKIKKRLK KENLLRIFSK TLAFLFLVLF ISFFVFLLTE ATKIGPDFAK SLFNLEFNLG NKQAGIWFPL LVSFIVSIGA LIIASYIGVR TSFFLVYRCK PKIRKKLSLI IDILSGIPSV IFGLFASQIL SIFFRDILKL PPLSLLNVIA MLSFMIIPIV ISLTTNTLTY VNNDLISVVV SLGENKTSAI YKIIKKEIKP QLTVILTLAF ARAISETMAV NFVLQSVNYQ EVINNNRFFT SDLKTLGSVI STFIFSENGD EQINGVLYIF GIIILILVSL LNFFAIWSAN PKTLERYPFL KKISNFIYQV VWFIPNNISA LFVDLTSTRQ SVKKIKVNNI NERSLFFKER LQSVVWIKLN YFLKIFQELI CTFLAFGFVL AILLFVFING SVAINNNGST VFSFEADSTG RALVNTLVII LITITITFPL ALLIAIWLNE YNNSKVVKNV FNFVIDSLSS MPSIIYGLFG LSFFLRVLQL SAGGANGTSL IAGILTISVV ILLFLIRTCQ QALNNVSWDL RISAFALGIS KREVIFKIVL PSALKGLIVA LILSINRIIA ETAPFFITSG LSSSNLFHLS LPGQTLTTRI YGQLFSINSN AISVMLETSL VSVVFLILLI FFSSYLIPSL FLLNKQKWLV IKSKFQSFKL WKRT // ID PTG3C_MYCGE Reviewed; 908 AA. AC P47315; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 123. DE RecName: Full=PTS system glucose-specific EIICBA component; DE AltName: Full=EII-Glc/EIII-Glc; DE AltName: Full=EIICBA-Glc; DE Includes: DE RecName: Full=Glucose permease IIC component; DE AltName: Full=PTS system glucose-specific EIIC component; DE Includes: DE RecName: Full=Glucose-specific phosphotransferase enzyme IIB component; DE EC=2.7.1.199; DE AltName: Full=PTS system glucose-specific EIIB component; DE Includes: DE RecName: Full=Glucose-specific phosphotransferase enzyme IIA component; DE AltName: Full=PTS system glucose-specific EIIA component; GN Name=ptsG; OrderedLocusNames=MG069; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 284-375. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [3] RP DISCUSSION OF SEQUENCE. RX PubMed=9689210; RA Reizer J., Paulsen I.T., Reizer A., Titgemeyer F., Saier M.H. Jr.; RT "Novel phosphotransferase system genes revealed by bacterial genome RT analysis: the complete complement of pts genes in Mycoplasma RT genitalium."; RL Microb. Comp. Genomics 1:151-164(1996). CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar CC phosphotransferase system (sugar PTS), a major carbohydrate active CC -transport system, catalyzes the phosphorylation of incoming sugar CC substrates concomitantly with their translocation across the cell CC membrane. This system is involved in glucose transport. CC -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D- CC glucose(Side 1) = [protein]-L-histidine + D-glucose 6- CC phosphate(Side 2). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00426}; Multi-pass membrane protein CC {ECO:0000255|PROSITE-ProRule:PRU00426}. CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel CC and contains the specific substrate-binding site. CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a CC cysteinyl or histidyl residue, depending on the transported sugar. CC Then, it transfers the phosphoryl group to the sugar substrate CC concomitantly with the sugar uptake processed by the EIIC domain. CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a CC histidyl residue. Then, it transfers the phosphoryl group to the CC EIIB domain. CC -!- SIMILARITY: Contains 1 PTS EIIA type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00416}. CC -!- SIMILARITY: Contains 1 PTS EIIB type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00421}. CC -!- SIMILARITY: Contains 1 PTS EIIC type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00426}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71287.1; -; Genomic_DNA. DR EMBL; U02207; AAD12499.1; -; Genomic_DNA. DR PIR; F64207; F64207. DR RefSeq; WP_009885925.1; NZ_AAGX01000011.1. DR ProteinModelPortal; P47315; -. DR STRING; 243273.MgenG_010200002836; -. DR EnsemblBacteria; AAC71287; AAC71287; MG_069. DR KEGG; mge:MG_069; -. DR PATRIC; 20009540; VBIMycGen98045_0079. DR eggNOG; ENOG4105CI1; Bacteria. DR eggNOG; COG1263; LUCA. DR eggNOG; COG1264; LUCA. DR eggNOG; COG2190; LUCA. DR KO; K02777; -. DR KO; K02778; -. DR KO; K02779; -. DR OMA; IFGYIER; -. DR OrthoDB; EOG6FFS9V; -. DR BioCyc; MGEN243273:GH2R-72-MONOMER; -. DR Proteomes; UP000000807; 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:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 3.30.1360.60; -; 1. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR018113; PTrfase_EIIB_Cys. DR InterPro; IPR001127; PTS_EIIA_1_perm. DR InterPro; IPR003352; PTS_EIIC. DR InterPro; IPR013013; PTS_EIIC_1. DR InterPro; IPR001996; PTS_IIB_1. DR Pfam; PF00358; PTS_EIIA_1; 1. DR Pfam; PF00367; PTS_EIIB; 1. DR Pfam; PF02378; PTS_EIIC; 2. DR SUPFAM; SSF51261; SSF51261; 1. DR SUPFAM; SSF55604; SSF55604; 1. DR TIGRFAMs; TIGR00826; EIIB_glc; 1. DR TIGRFAMs; TIGR00830; PTBA; 1. DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1. DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1. DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1. DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Kinase; Membrane; KW Phosphotransferase system; Reference proteome; Sugar transport; KW Transferase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 908 PTS system glucose-specific EIICBA FT component. FT /FTId=PRO_0000186559. FT TRANSMEM 31 51 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 71 91 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 100 120 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 155 175 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 189 209 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 459 479 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 487 507 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 509 529 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 536 556 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT TRANSMEM 571 591 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00426}. FT DOMAIN 1 264 PTS EIIC type-1; first part. FT {ECO:0000255|PROSITE-ProRule:PRU00426}. FT DOMAIN 451 602 PTS EIIC type-1; second part. FT {ECO:0000255|PROSITE-ProRule:PRU00426}. FT DOMAIN 631 713 PTS EIIB type-1. {ECO:0000255|PROSITE- FT ProRule:PRU00421}. FT DOMAIN 762 875 PTS EIIA type-1. {ECO:0000255|PROSITE- FT ProRule:PRU00416}. FT REGION 265 450 Unknown. FT ACT_SITE 653 653 Phosphocysteine intermediate; for EIIB FT activity. {ECO:0000255|PROSITE- FT ProRule:PRU00421}. FT ACT_SITE 815 815 Tele-phosphohistidine intermediate; for FT EIIA activity. {ECO:0000255|PROSITE- FT ProRule:PRU00416}. SQ SEQUENCE 908 AA; 98399 MW; A079970CF625D9E5 CRC64; MQISLVKIRN KFKQRNRGSF RQWVGKLSNG LMIPIAVLPL AGIFLGIGDA ISSNSSGIVG VKFFGEFIKQ GGNVVFANLP ILFAVAIAIT FSQDAGVAGF SAFVFWATMN AFMSSLIIPV DANNTASGYN ILYWKAVPQS AIASTLGLNS LSTSVFGGII VGALTAYLYN KFYAIRLPDV IGFFSGTRFV PIICMTIAIP VALLLLMVWP GVSILLNLIG TGLGILGGRG YGANSLIFGY IERALIPFGV HHAFYAPLWY TSAGGSLQEI ANQQVWIRAP GSDYVTRVIG WEDFNTPGKW VIPAALANGT SGMMNGATTT GQDSTSALSK YMSKESTNFL SWKELVDGLT RKGNFDELAK NGLLDGSNKI WIGLNQSGIL GKKVLLSDGK DYTITFKTFA NTTPTFWSHG AHALLPISGT PSAITNGVTV NGTANSKTYN VSQFTVAVPS LNPAQYSQGK FPFMLIGIPA AGLAMILAAP KGRRKEASSI IGSAAFTSFL TGITEPFEFT FLFLAPWLFY GIHAVLAAVS FWLMNLLSAN VGQTFSGSFI DFILYGALPD GRGWLANSYL VPIIGIFLAL IYFPTFYFLT IRFNLATPGR GGKLITKKEY LAAKAAQKTD QTTNTNFNQT QIEAGMLLRA YGGSENIAEL GACITKLRVT VKNPELVNET IIKDLGAAGV MRTTPTFFVA VFGTRAAVYK SAMQDIIQGK VNWTELQKVL DKNDSTVEKP EIKPTPVLKV QDEIVILSPV NGTLKPLTQV PDDTFKNRLV GDGIAILPSD GHFKAPGDVG VKTELAFPTG HAFIFDVDGV KVMLHIGIDT VKINADKKPG EQLEVFDVKT KQGEYTKLKS ESVVEVDLKK LKRKYDPITP FIVMQESLDN FKLVPIRQRG EIKVGQPLFK LIYKDKKS // ID PSTB_MYCGE Reviewed; 329 AA. AC P47650; Q49513; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 117. 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}; OrderedLocusNames=MG410; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-313. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 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; L43967; AAC71638.1; -; Genomic_DNA. DR EMBL; U01707; AAB01019.1; -; Genomic_DNA. DR PIR; D64245; D64245. DR RefSeq; WP_009885613.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47650; -. DR STRING; 243273.MgenG_010200000440; -. DR EnsemblBacteria; AAC71638; AAC71638; MG_410. DR KEGG; mge:MG_410; -. DR PATRIC; 20010412; VBIMycGen98045_0479. DR eggNOG; ENOG4105BZY; Bacteria. DR eggNOG; COG1117; LUCA. DR KO; K02036; -. DR OMA; FDKPKFQ; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-467-MONOMER; -. DR Proteomes; UP000000807; 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 membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Phosphate transport; Reference proteome; KW Transport. FT CHAIN 1 329 Phosphate import ATP-binding protein FT PstB. FT /FTId=PRO_0000092840. FT DOMAIN 83 325 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01702}. FT NP_BIND 116 123 ATP. {ECO:0000255|HAMAP-Rule:MF_01702}. FT CONFLICT 310 329 KQIFTKPKQKATNSYISGKN -> NRYL (in Ref. 2; FT AAB01019). {ECO:0000305}. SQ SEQUENCE 329 AA; 37940 MW; C021505065B933D3 CRC64; MEKNIKALWK NFQLKLEKIK HYRKLYEQQI KEYKKKITGL NNETDANEIS RIKNEIEILN RLIKIKNTKD NVIKKDFDEK NVFEIRNFNF WYNKNKQVLF DINLDIKRNK ITALIGKSGC GKSTFIRCLN KLNDLNENTR WTGDIYFLGK NINSGIINDL TLRTSVGMVF QKLTPFNFSI FENIAYGIRA HGIHNKNAIN EIVRQALISA ALWDEVKDNL HRNANTLSGG QQQRLCIARA IALQPDVLLM DEPTSALDSI ATNSIELLIQ QLKEKFTIVI VTHSMAQTIR ITDETIFFAD GRVIEQGTTK QIFTKPKQKA TNSYISGKN // ID PTHP_MYCGE Reviewed; 88 AA. AC P47287; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Phosphocarrier protein HPr; DE EC=2.7.11.-; DE AltName: Full=Histidine-containing protein; GN Name=ptsH; OrderedLocusNames=MG041; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP DISCUSSION OF SEQUENCE. RX PubMed=9689210; RA Reizer J., Paulsen I.T., Reizer A., Titgemeyer F., Saier M.H. Jr.; RT "Novel phosphotransferase system genes revealed by bacterial genome RT analysis: the complete complement of pts genes in Mycoplasma RT genitalium."; RL Microb. Comp. Genomics 1:151-164(1996). CC -!- FUNCTION: General (non sugar-specific) component of the CC phosphoenolpyruvate-dependent sugar phosphotransferase system CC (sugar PTS). This major carbohydrate active-transport system CC catalyzes the phosphorylation of incoming sugar substrates CC concomitantly with their translocation across the cell membrane. CC The phosphoryl group from phosphoenolpyruvate (PEP) is transferred CC to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr CC then transfers it to the permease (enzymes II/III) (By CC similarity). {ECO:0000250}. CC -!- FUNCTION: P-Ser-HPr interacts with the catabolite control protein CC A (CcpA), forming a complex that binds to DNA at the catabolite CC response elements cre, operator sites preceding a large number of CC catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in CC carbon catabolite repression (CCR), a mechanism that allows CC bacteria to coordinate and optimize the utilization of available CC carbon sources. P-Ser-HPr also plays a role in inducer exclusion, CC in which it probably interacts with several non-PTS permeases and CC inhibits their transport activity (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein HPr N(pi)-phospho-L-histidine + CC protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L- CC histidine. CC -!- ENZYME REGULATION: Phosphorylation on Ser-47 inhibits the CC phosphoryl transfer from enzyme I to HPr. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HPr domain. {ECO:0000255|PROSITE- CC ProRule:PRU00681}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71257.1; -; Genomic_DNA. DR PIR; E64204; E64204. DR RefSeq; WP_010869302.1; NC_000908.2. DR ProteinModelPortal; P47287; -. DR STRING; 243273.MgenG_010200001050; -. DR EnsemblBacteria; AAC71257; AAC71257; MG_041. DR KEGG; mge:MG_041; -. DR PATRIC; 20009460; VBIMycGen98045_0040. DR eggNOG; ENOG41082BZ; Bacteria. DR eggNOG; COG1925; LUCA. DR KO; K11189; -. DR OMA; EYTIQDP; -. DR OrthoDB; EOG6XDGX2; -. DR BioCyc; MGEN243273:GH2R-41-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase 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; 3.30.1340.10; -; 1. DR InterPro; IPR000032; HPr_prot-like. DR InterPro; IPR001020; PTS_HPr_His_P_site. DR InterPro; IPR002114; PTS_HPr_Ser_P_site. DR Pfam; PF00381; PTS-HPr; 1. DR PRINTS; PR00107; PHOSPHOCPHPR. DR SUPFAM; SSF55594; SSF55594; 1. DR TIGRFAMs; TIGR01003; PTS_HPr_family; 1. DR PROSITE; PS51350; PTS_HPR_DOM; 1. DR PROSITE; PS00369; PTS_HPR_HIS; 1. DR PROSITE; PS00589; PTS_HPR_SER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Kinase; Phosphoprotein; KW Phosphotransferase system; Reference proteome; KW Serine/threonine-protein kinase; Sugar transport; Transcription; KW Transcription regulation; Transferase; Transport. FT CHAIN 1 88 Phosphocarrier protein HPr. FT /FTId=PRO_0000107863. FT DOMAIN 1 88 HPr. {ECO:0000255|PROSITE- FT ProRule:PRU00681}. FT ACT_SITE 15 15 Pros-phosphohistidine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU00681}. FT MOD_RES 47 47 Phosphoserine; by HPrK/P. FT {ECO:0000255|PROSITE-ProRule:PRU00681}. SQ SEQUENCE 88 AA; 9410 MW; C314E01CEF3803B7 CRC64; MKKFQAVIKD PVGIHARPAS ILASEASKFK SELKLVAPSG VEGNIKSIIN LMSLGIRHND NITIKADGAD EEEALAAIKA CLEKNKVI // ID PT1_MYCGE Reviewed; 572 AA. AC P47668; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase; DE EC=2.7.3.9; DE AltName: Full=Phosphotransferase system, enzyme I; GN Name=ptsI; OrderedLocusNames=MG429; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP DISCUSSION OF SEQUENCE. RX PubMed=9689210; RA Reizer J., Paulsen I.T., Reizer A., Titgemeyer F., Saier M.H. Jr.; RT "Novel phosphotransferase system genes revealed by bacterial genome RT analysis: the complete complement of pts genes in Mycoplasma RT genitalium."; RL Microb. Comp. Genomics 1:151-164(1996). CC -!- FUNCTION: General (non sugar-specific) component of the CC phosphoenolpyruvate-dependent sugar phosphotransferase system CC (sugar PTS). This major carbohydrate active-transport system CC catalyzes the phosphorylation of incoming sugar substrates CC concomitantly with their translocation across the cell membrane. CC Enzyme I transfers the phosphoryl group from phosphoenolpyruvate CC (PEP) to the phosphoryl carrier protein (HPr) (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + protein L-histidine = CC pyruvate + protein N(pi)-phospho-L-histidine. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DOMAIN: The N-terminal domain contains the HPr binding site, the CC central domain the pyrophosphate/phosphate carrier histidine, and CC the C-terminal domain the pyruvate binding site. {ECO:0000250}. CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated CC by a phosphocarrier histidine residue located on the surface of CC the central domain. The two first partial reactions are catalyzed CC at an active site located on the N-terminal domain, and the third CC partial reaction is catalyzed at an active site located on the C- CC terminal domain. For catalytic turnover, the central domain CC swivels from the concave surface of the N-terminal domain to that CC of the C-terminal domain (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme 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; L43967; AAC72450.1; -; Genomic_DNA. DR PIR; D64247; D64247. DR RefSeq; WP_010869480.1; NC_000908.2. DR ProteinModelPortal; P47668; -. DR EnsemblBacteria; AAC72450; AAC72450; MG_429. DR KEGG; mge:MG_429; -. DR PATRIC; 20010444; VBIMycGen98045_0495. DR KO; K08483; -. DR OMA; NIEIGIM; -. DR OrthoDB; EOG657JBQ; -. DR BioCyc; MGEN243273:GH2R-483-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 1.10.274.10; -; 1. DR Gene3D; 3.20.20.60; -; 1. DR Gene3D; 3.50.30.10; -; 1. 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; IPR024692; PTS_EI. DR InterPro; IPR006318; PTS_EI-like. DR InterPro; IPR008731; PTS_EIN. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR Pfam; PF05524; PEP-utilisers_N; 1. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF02896; PEP-utilizers_C; 1. DR PIRSF; PIRSF000732; PTS_enzyme_I; 1. DR SUPFAM; SSF47831; SSF47831; 1. DR SUPFAM; SSF51621; SSF51621; 1. DR SUPFAM; SSF52009; SSF52009; 1. DR TIGRFAMs; TIGR01417; PTS_I_fam; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding; KW Phosphotransferase system; Reference proteome; Sugar transport; KW Transferase; Transport. FT CHAIN 1 572 Phosphoenolpyruvate-protein FT phosphotransferase. FT /FTId=PRO_0000147076. FT ACT_SITE 190 190 Tele-phosphohistidine intermediate. FT {ECO:0000250}. FT ACT_SITE 498 498 Proton donor. {ECO:0000250}. FT METAL 427 427 Magnesium. {ECO:0000250}. FT METAL 451 451 Magnesium. {ECO:0000250}. FT BINDING 297 297 Substrate. {ECO:0000250}. FT BINDING 333 333 Substrate. {ECO:0000250}. FT BINDING 427 427 Substrate. {ECO:0000250}. FT BINDING 448 448 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 449 449 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 450 450 Substrate. {ECO:0000250}. FT BINDING 451 451 Substrate; via amide nitrogen. FT {ECO:0000250}. SQ SEQUENCE 572 AA; 64202 MW; DFCB4E00589A940E CRC64; MKKIIGIGVS DGIAVAKAFI IQTPQFDVKK YTNVKMTPTQ AKKLLSSAFQ KAKKDLEEIK TITVKNINQE AGMIFDAHIQ ILNDPTITEQ LEQQLNKNIH PVIAVDNVFQ QTALMFSEMD DKYFKERASD ILDLHQRLLS YLTGVKLNDL IRIKSDVIIV ANDLTPSQTA TLNKKYVKGF LTESGGKTSH AAIMARSMEI PAIVGLKNIT SKVEDGKTVG INGRKGIVGF DFSSKDITQW KQEKELESNF QNELKQYTNK LVKTLDGYEV IVASNIGNVK DMDLAVEYNT NGIGLFRTEF LYMSSQDWPD ESVQFEAYKT VLQKAKNDLV IIRTLDIGGD KKLNYFQFPH EDNPFLGYRA IRLTLDKQAV FKTQLRALLR ASDYGNLGIM FPMVATLDEL VQVKQLLTKV QQEFNETKKF KLGIMIEIPS AALAADCLGK HVDFFSIGSN DLIQYSFAAD RMNKNVSYLY QPLNPALLRL IKLVVEGGKL NNVWTGMCGE MASDQYAIPL LLGLGLTELS MSASSMFKAR MVIAKITINE CKSLVEKALK LTSDSAVRKL VENFFKKKNI FI // ID PTAS_MYCGE Reviewed; 320 AA. AC P47541; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 92. DE RecName: Full=Phosphate acetyltransferase; DE EC=2.3.1.8; DE AltName: Full=Phosphotransacetylase; GN Name=pta; OrderedLocusNames=MG299; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + phosphate = CoA + acetyl CC phosphate. CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA CC biosynthesis; acetyl-CoA from acetate: step 2/2. 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; L43967; AAC71521.1; -; Genomic_DNA. DR PIR; A64233; A64233. DR RefSeq; WP_009885878.1; NZ_AAGX01000008.1. DR ProteinModelPortal; P47541; -. DR STRING; 243273.MgenG_010200002469; -. DR EnsemblBacteria; AAC71521; AAC71521; MG_299. DR KEGG; mge:MG_299; -. DR PATRIC; 20010128; VBIMycGen98045_0350. DR eggNOG; ENOG4107ZCE; Bacteria. DR eggNOG; COG0280; LUCA. DR KO; K00625; -. DR OMA; GVFIMAR; -. DR OrthoDB; EOG6BKJ5W; -. DR BioCyc; MGEN243273:GH2R-335-MONOMER; -. DR UniPathway; UPA00340; UER00459. DR Proteomes; UP000000807; 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; IPR004614; P_AcTrfase. DR InterPro; IPR002505; PTA_PTB. DR Pfam; PF01515; PTA_PTB; 1. DR PIRSF; PIRSF000428; P_Ac_trans; 1. DR TIGRFAMs; TIGR00651; pta; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Reference proteome; KW Transferase. FT CHAIN 1 320 Phosphate acetyltransferase. FT /FTId=PRO_0000179133. SQ SEQUENCE 320 AA; 35469 MW; 9091249E1661A888 CRC64; MSVIDIFKKR LQAVSKKPVI IFPEGWSASV LKAVEMLNES KLIQPAVIFH NRQEIPANFD KKITHYVIDE MDLTSYANFV YEKRKHKGMD LKEAQKFVRD PSSLAATLVA LKVVDGEVCG KEYATKDTLR PALQLLATGN FVSSVFIMEK GEERLYFTDC AFAVYPNSQE LATIAENTFN FAKSLNEDEI KMAFLSYSTL GSGKGEMVDK VVLATKLFLE KHPELHQSVC GELQFDAAFV EKVRLQKAPQ LTWKNSANIY VFPNLDAGNI AYKIAQRLGG YDAIGPIVLG LSSPVNDLSR GASVSDIFNV GIITAAQAIK // ID PTF3A_MYCGE Reviewed; 680 AA. AC P47308; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 120. DE RecName: Full=PTS system fructose-specific EIIABC component; DE AltName: Full=EIIABC-Fru; DE Includes: DE RecName: Full=Fructose-specific phosphotransferase enzyme IIA component; DE AltName: Full=EII-Fru; DE AltName: Full=PTS system fructose-specific EIIA component; DE Includes: DE RecName: Full=Fructose-specific phosphotransferase enzyme IIB component; DE EC=2.7.1.202; DE AltName: Full=EIII-Fru; DE AltName: Full=PTS system fructose-specific EIIB component; DE Includes: DE RecName: Full=Fructose permease IIC component; DE AltName: Full=PTS system fructose-specific EIIC component; GN Name=fruA; OrderedLocusNames=MG062; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-253. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [3] RP DISCUSSION OF SEQUENCE. RX PubMed=9689210; RA Reizer J., Paulsen I.T., Reizer A., Titgemeyer F., Saier M.H. Jr.; RT "Novel phosphotransferase system genes revealed by bacterial genome RT analysis: the complete complement of pts genes in Mycoplasma RT genitalium."; RL Microb. Comp. Genomics 1:151-164(1996). CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar CC phosphotransferase system (sugar PTS), a major carbohydrate active CC -transport system, catalyzes the phosphorylation of incoming sugar CC substrates concomitantly with their translocation across the cell CC membrane. This system is involved in fructose transport. CC -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D- CC fructose(Side 1) = [protein]-L-histidine + D-fructose 1- CC phosphate(Side 2). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00427}; Multi-pass membrane protein CC {ECO:0000255|PROSITE-ProRule:PRU00427}. CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a CC histidyl residue. Then, it transfers the phosphoryl group to the CC EIIB domain. CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a CC cysteinyl or histidyl residue, depending on the transported sugar. CC Then, it transfers the phosphoryl group to the sugar substrate CC concomitantly with the sugar uptake processed by the EIIC domain. CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel CC and contains the specific substrate-binding site. CC -!- SIMILARITY: Contains 1 PTS EIIA type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00417}. CC -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00422}. CC -!- SIMILARITY: Contains 1 PTS EIIC type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00427}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71279.1; -; Genomic_DNA. DR EMBL; U02138; AAD12415.1; -; Genomic_DNA. DR PIR; H64206; H64206. DR RefSeq; WP_010869312.1; NC_000908.2. DR ProteinModelPortal; P47308; -. DR STRING; 243273.MgenG_010200001210; -. DR EnsemblBacteria; AAC71279; AAC71279; MG_062. DR KEGG; mge:MG_062; -. DR PATRIC; 20009508; VBIMycGen98045_0063. DR eggNOG; ENOG4105DM4; Bacteria. DR eggNOG; COG1299; LUCA. DR eggNOG; COG1445; LUCA. DR eggNOG; COG1762; LUCA. DR KO; K02768; -. DR KO; K02769; -. DR KO; K02770; -. DR OMA; TIHLNIE; -. DR OrthoDB; EOG6XDGX2; -. DR BioCyc; MGEN243273:GH2R-65-MONOMER; -. DR Proteomes; UP000000807; 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:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro. DR GO; GO:0005351; F:sugar:proton symporter activity; IEA:InterPro. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 3.40.930.10; -; 1. DR InterPro; IPR016152; PTrfase/Anion_transptr. DR InterPro; IPR002178; PTS_EIIA_type-2_dom. DR InterPro; IPR013011; PTS_EIIB_2. DR InterPro; IPR003501; PTS_EIIB_2/3. DR InterPro; IPR003352; PTS_EIIC. DR InterPro; IPR013014; PTS_EIIC_2. DR InterPro; IPR004715; PTS_IIA_fruc. DR InterPro; IPR003353; PTS_IIB_fruc. DR InterPro; IPR006327; PTS_IIC_fruc. DR Pfam; PF00359; PTS_EIIA_2; 1. DR Pfam; PF02378; PTS_EIIC; 1. DR Pfam; PF02302; PTS_IIB; 1. DR SUPFAM; SSF52794; SSF52794; 1. DR SUPFAM; SSF55804; SSF55804; 1. DR TIGRFAMs; TIGR00829; FRU; 1. DR TIGRFAMs; TIGR00848; fruA; 1. DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1. DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1. DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1. DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Kinase; Membrane; KW Phosphotransferase system; Reference proteome; Sugar transport; KW Transferase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 680 PTS system fructose-specific EIIABC FT component. FT /FTId=PRO_0000186510. FT TRANSMEM 306 326 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 352 372 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 377 397 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 410 430 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 449 469 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 488 508 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 530 550 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 565 585 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 590 610 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 643 663 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT DOMAIN 4 149 PTS EIIA type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00417}. FT DOMAIN 168 264 PTS EIIB type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00422}. FT DOMAIN 298 675 PTS EIIC type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT ACT_SITE 68 68 Tele-phosphohistidine intermediate; for FT EIIA activity. {ECO:0000255|PROSITE- FT ProRule:PRU00417}. FT ACT_SITE 174 174 Phosphocysteine intermediate; for EIIB FT activity. {ECO:0000250}. SQ SEQUENCE 680 AA; 74090 MW; A6AC1B1D7AAA9DA4 CRC64; MFKNLLRPSL FFNWSQKTFK NKFSFLKQAA NALQKQAVIN DNNVAFEALK KREEEITTGI ITSLALPHLQ SQSVIEPFVA VFKVKNLDWQ SLDQKPVKLI FLIGVLVDKT NLHLDFISNF SKLMLNETFA SKVLNVTSYN GLIKLIDLFN QQKVQDQPAV ETKKEYDFVA VTACPTGIAH TFMAKEALEA FAKKHNLYVK VETQGTDGIQ NQLTSDDINN AKGVILACDR LIDFSRFYAN KNVIEVSTTK AIKKPDEVYE LIKNQKGKQL ANSAKPTNQT QLAESEGEFN FNNFHKRIYR AILSGVSYML PFVVFGGILI ALSFLIDINN ANNAGGNFGT INPVANWLNK LGGISFSLIV PILSAYIAYA LVSRQGLLPG FVVGLISSGQ FLLNIVLTNG TIEWLAPSQV SSGFFGAIFG GLLSACLIIV QQNYIYKKLP QSLQGIKNIL FIPLFGTLFT AGLFWVINIP LIYLNYGLSL FLNIMNSPIL APLLGFVIGL MMCFDLGGPI NKAAYVFGVV SLQNQNAGTI SMAAAMLSGM VPPLSIALAA SIRKSCFDKQ ELPAAYACYL MGLSFISEGA IPFVVKKPKV MLTANLIAGA ICGALTGAFA LSIRAPHGGV FVFALLKTTL QGIEGATLQT GVGIGLALVC LIISMIVGSS IIIGYDLIAK HNQRKQNLNS // ID PTH_MYCGE Reviewed; 189 AA. AC P47329; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 96. 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=MG083; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-189. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71301.1; -; Genomic_DNA. DR EMBL; U02185; AAD12470.1; -; Genomic_DNA. DR PIR; B64209; B64209. DR RefSeq; WP_009885642.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47329; -. DR STRING; 243273.MgenG_010200000625; -. DR EnsemblBacteria; AAC71301; AAC71301; MG_083. DR KEGG; mge:MG_083; -. DR PATRIC; 20009568; VBIMycGen98045_0093. DR eggNOG; ENOG4108ZPD; Bacteria. DR eggNOG; COG0193; LUCA. DR KO; K01056; -. DR OMA; FSPKHNA; -. DR OrthoDB; EOG6C5RTR; -. DR BioCyc; MGEN243273:GH2R-86-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-HAMAP. 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 1 189 Peptidyl-tRNA hydrolase. FT /FTId=PRO_0000187771. SQ SEQUENCE 189 AA; 21833 MW; 34F28B201DF55965 CRC64; MPTYKLIVGL GNLGKKYEKT RHNAGFMVLD RLASLFHLNF DKTNKLGDYL FIKEKAAILA KPATFMNNSG LFVKWLQDHF QIPLANIMIV HDEIAFDLGV IRLKMQGSAN NHNGIKSVIR HLDTEQFNRL RFGIKSQNTS NILHEQVMSE FQNSELTKLE VAITKSVELL KRYIEGEELQ RLMEYYHHG // ID RBGA_MYCGE Reviewed; 270 AA. AC Q49435; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Probable ribosome biogenesis GTPase A; GN Name=rbgA; OrderedLocusNames=MG442; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. 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; L43967; AAC72462.1; -; Genomic_DNA. DR PIR; H64248; H64248. DR ProteinModelPortal; Q49435; -. DR STRING; 243273.MgenG_010200000250; -. DR EnsemblBacteria; AAC72462; AAC72462; MG_442. DR KEGG; mge:MG_442; -. DR PATRIC; 20010470; VBIMycGen98045_0508. DR eggNOG; ENOG4105C9W; Bacteria. DR eggNOG; COG1161; LUCA. DR KO; K14540; -. DR OMA; ARCPISS; -. DR OrthoDB; EOG6G4VXH; -. DR BioCyc; MGEN243273:GH2R-495-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Hydrolase; KW Nucleotide-binding; Reference proteome; Ribosome biogenesis. FT CHAIN 1 270 Probable ribosome biogenesis GTPase A. FT /FTId=PRO_0000210614. FT DOMAIN 20 174 CP-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01058}. FT NP_BIND 126 131 GTP. {ECO:0000250}. FT BINDING 170 170 GTP; via amide nitrogen. {ECO:0000250}. SQ SEQUENCE 270 AA; 30897 MW; 16B9072A2E83763E CRC64; MDTYTSAKIN WFPGHMKKIH DQLKKLSSQI DGIIEIVDAR APTLTHNSEI ISYFLNKPKL ILALKTDLAQ YKPNKKILFG SLKEPFKLKK KVLKTLTTLF ANKRQQLKAK GLLIKQFRLA VIGMPNVGKS SLINLLINKN HLKVANRAGI TKSLNWIQIS PELLLSDTPG VFLKRIDEIQ IGYKLVLTNV IRREVVNIEE VGMFAFNYLK KHYKQLLPFE ADSFINFLEK FAKVRGLIKK ANELNTNLAC EIFINELING KYGKLSYELN // ID PYRH_MYCGE Reviewed; 243 AA. AC P47672; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 3. DT 13-APR-2016, entry version 99. 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}; Synonyms=smbA; GN OrderedLocusNames=MG434; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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: Inhibited by UTP. {ECO:0000255|HAMAP- CC 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; L43967; AAC72455.1; -; Genomic_DNA. DR PIR; T09769; T09769. DR RefSeq; WP_009885599.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47672; -. DR STRING; 243273.MgenG_010200000290; -. DR EnsemblBacteria; AAC72455; AAC72455; MG_434. DR KEGG; mge:MG_434; -. DR PATRIC; 20010454; VBIMycGen98045_0500. DR eggNOG; ENOG4105C41; Bacteria. DR eggNOG; COG0528; LUCA. DR KO; K09903; -. DR OMA; IIVFDMN; -. DR OrthoDB; EOG6M0T8S; -. DR BioCyc; MGEN243273:GH2R-488-MONOMER; -. DR UniPathway; UPA00159; UER00275. DR Proteomes; UP000000807; 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 ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 243 Uridylate kinase. FT /FTId=PRO_0000143859. FT NP_BIND 15 18 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT NP_BIND 138 145 UMP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 56 56 UMP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 57 57 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 61 61 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 166 166 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 172 172 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01220}. FT BINDING 175 175 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. SQ SEQUENCE 243 AA; 26735 MW; 675AC6240FA47E65 CRC64; MHKSNNKIRQ RIIIKLSGAG LTKENSQPFS NDFFETIINQ LKVLKESYQV GIVIGGGNII RGNNCQEFNI AEYHGHQLGI IATVVNGYFL KAKLDAHNLK SALLSAISCP SLAVQILSQQ TIDKAFEEND FVIFSGGTGN PYFSTDTALA LRAVQTKAVA ILIGKNGVDG VYTADPKKDK NATFLPTLNY DHAIKNDLKI MDITAFTMCK ENNLKIIIFN INAENALLDA LNKKGRFTII ENN // ID RECA_MYCGE Reviewed; 340 AA. AC P47581; Q49512; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 102. 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}; OrderedLocusNames=MG339; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-124. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71564.1; -; Genomic_DNA. DR EMBL; U01704; AAB01016.1; -; Genomic_DNA. DR PIR; E64237; E64237. DR RefSeq; WP_009885970.1; NZ_AAGX01000014.1. DR ProteinModelPortal; P47581; -. DR STRING; 243273.MgenG_010200003136; -. DR EnsemblBacteria; AAC71564; AAC71564; MG_339. DR KEGG; mge:MG_339; -. DR PATRIC; 20010238; VBIMycGen98045_0396. DR eggNOG; ENOG4105C68; Bacteria. DR eggNOG; COG0468; LUCA. DR KO; K03553; -. DR OMA; TRKGAWY; -. DR OrthoDB; EOG6ZKXNZ; -. DR BioCyc; MGEN243273:GH2R-389-MONOMER; -. DR Proteomes; UP000000807; 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:UniProtKB-HAMAP. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003697; F:single-stranded DNA binding; 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; 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA damage; KW DNA recombination; DNA repair; DNA-binding; Nucleotide-binding; KW Reference proteome; SOS response. FT CHAIN 1 340 Protein RecA. FT /FTId=PRO_0000122758. FT NP_BIND 67 74 ATP. {ECO:0000255|HAMAP-Rule:MF_00268}. FT CONFLICT 32 36 AKKNS -> CKEKH (in Ref. 2; AAB01016). FT {ECO:0000305}. SQ SEQUENCE 340 AA; 37430 MW; 0957B712CD2125C0 CRC64; MAQKEIINKK NTQKNSSFIE SNNLTSFDFF DAKKNSEIET ISTGSLNLDE ALGSGGLPLG RIVELYGNES SGKTTIALNA VASFQKAGKT ACYIDAEGAL DLAYAKSIGI DLNKLLIAHP RHGENAFALI ESLIKTNKIS LIVIDSVAAL IPKQELEGTI EEQTIGLHAR MMSKGLRRIQ SILPDSKTCV LFINQLREKP GVMFGNNEVT TGGKALRFYS SLRMEAKRVE LLKDKFNNYV GIKTKVMVSK NKIAKPFGVA ILEIMFNRGF VHEHEVIDLA LKFNVVVRAG NSYSFNNESI AVGKEKLLNV LSEKPALFEQ IKELTVQQLA NKNSFQQTAS // ID RF1_MYCGE Reviewed; 359 AA. AC P47500; Q49455; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Peptide chain release factor 1; DE Short=RF-1; GN Name=prfA; OrderedLocusNames=MG258; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 241-353. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71478.1; -; Genomic_DNA. DR EMBL; U01800; AAD12326.1; -; Genomic_DNA. DR PIR; E64228; E64228. DR RefSeq; WP_009885793.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47500; -. DR STRING; 243273.MgenG_010200001777; -. DR EnsemblBacteria; AAC71478; AAC71478; MG_258. DR KEGG; mge:MG_258; -. DR PATRIC; 20010004; VBIMycGen98045_0295. DR eggNOG; ENOG4105C8K; Bacteria. DR eggNOG; COG0216; LUCA. DR KO; K02835; -. DR OMA; LRIDVFC; -. DR OrthoDB; EOG6TN48J; -. DR BioCyc; MGEN243273:GH2R-283-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-HAMAP. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methylation; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 359 Peptide chain release factor 1. FT /FTId=PRO_0000177702. FT MOD_RES 236 236 N5-methylglutamine. {ECO:0000250}. FT CONFLICT 350 353 KKQQ -> RTQL (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 359 AA; 40808 MW; 3DBF7D8E40E43A7C CRC64; MDFDKQLFFN VEKIVELTEQ LEKDLNKPNL SFEQIKVINK ELKHKQPLIV KFKELQKLVE NANEAEQILN NSSLKELHEE AKKELEKIKA SLPSLEEEIK FLLLPVDENN QKNVIVEIRP AAGGDESCIF LSDLFNMYKN YCTSKNWTVE LNEIIPASVG INFVSFAVNG TDVFAKLKFE SGVHRVQRVP LTEAKGRVHT STVTVAVLPQ LEEVEITINP SDLRIDTYRA SGAGGQHVNR TESAVRITHL PTGIVVACQE GKSQFSNRDK AMKMLRAKLW ENAQNKQLST QADLRKSQVG SGERAEKIRT YNYPQNRITD HRIKLTINKL NTVILGDLDE IIEALQADEK KQQLEKFIS // ID RBFA_MYCGE Reviewed; 112 AA. AC P47389; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003}; GN Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; OrderedLocusNames=MG143; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71361.1; -; Genomic_DNA. DR PIR; H64215; H64215. DR RefSeq; WP_009885829.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47389; -. DR SMR; P47389; 6-101. DR STRING; 243273.MgenG_010200002074; -. DR EnsemblBacteria; AAC71361; AAC71361; MG_143. DR KEGG; mge:MG_143; -. DR PATRIC; 20009716; VBIMycGen98045_0164. DR eggNOG; COG0858; LUCA. DR KO; K02834; -. DR OMA; NRTIINE; -. DR OrthoDB; EOG6XQ3TJ; -. DR BioCyc; MGEN243273:GH2R-151-MONOMER; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; rRNA processing. FT CHAIN 1 112 Ribosome-binding factor A. FT /FTId=PRO_0000102692. SQ SEQUENCE 112 AA; 12907 MW; 201F7B6D236EF3DB CRC64; MASYRKQRIE NDIIRLINRT IINEIYDPVV KLGHVSHVKL SADFFHAVVY LDCYDRSQIQ TVVNAFKKAQ GVFSQMLAQN LYLAKSVKLH FVKDDAIDNA LKIEQIINSL KN // ID RECU_MYCGE Reviewed; 166 AA. AC Q49422; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Holliday junction resolvase RecU; DE EC=3.1.22.-; DE AltName: Full=Recombination protein U homolog; GN Name=recU; OrderedLocusNames=MG352; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Endonuclease that resolves Holliday junction CC intermediates in genetic recombination. Cleaves mobile four-strand CC junctions by introducing symmetrical nicks in paired strands. CC Promotes annealing of linear ssDNA with homologous dsDNA. Required CC for DNA repair, homologous recombination and chromosome CC segregation (By similarity). {ECO:0000250}. 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RecU 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; L43967; AAC71577.1; -; Genomic_DNA. DR PIR; I64238; I64238. DR RefSeq; WP_009885810.1; NZ_AAGX01000006.1. DR ProteinModelPortal; Q49422; -. DR STRING; 243273.MgenG_010200001898; -. DR EnsemblBacteria; AAC71577; AAC71577; MG_352. DR KEGG; mge:MG_352; -. DR PATRIC; 20010280; VBIMycGen98045_0414. DR eggNOG; ENOG4108UI2; Bacteria. DR eggNOG; COG3331; LUCA. DR KO; K03700; -. DR OrthoDB; EOG6W19NP; -. DR BioCyc; MGEN243273:GH2R-406-MONOMER; -. DR BRENDA; 3.1.22.4; 3528. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004519; F:endonuclease 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:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1350.10; -; 1. DR HAMAP; MF_00130; RecU; 1. DR InterPro; IPR004612; Resolv_RecU. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR Pfam; PF03838; RecU; 1. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR00648; recU; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA damage; DNA recombination; KW DNA repair; Endonuclease; Hydrolase; Magnesium; Metal-binding; KW Nuclease; Reference proteome. FT CHAIN 1 166 Holliday junction resolvase RecU. FT /FTId=PRO_0000212318. FT METAL 57 57 Magnesium. {ECO:0000250}. FT METAL 70 70 Magnesium. {ECO:0000250}. FT METAL 88 88 Magnesium. {ECO:0000250}. FT SITE 72 72 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 166 AA; 19382 MW; 6ACB82A007156C76 CRC64; MINANRGMLL ETIVNQTIAR LKDHPDIWLE KRFLPIKPIA FRHAHVSGNV SQKSKTDYYG IYKGMYFDFE AKQTNKSNFP IAQIAEHQLN HLKRIDQIGG VSFLLIYFQT KDQIFAFHTK DLLETIKNQE SKTIKRELIE QKSQKVPLLY PGIIDLISII QSFKNY // ID RIBF_MYCGE Reviewed; 269 AA. AC P47391; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=Putative riboflavin biosynthesis protein RibF; DE Includes: DE RecName: Full=Riboflavin kinase; DE EC=2.7.1.26; DE AltName: Full=Flavokinase; DE Includes: DE RecName: Full=FMN adenylyltransferase; DE EC=2.7.7.2; DE AltName: Full=FAD pyrophosphorylase; DE AltName: Full=FAD synthase; GN Name=ribF; OrderedLocusNames=MG145; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- CATALYTIC ACTIVITY: ATP + riboflavin = ADP + FMN. CC -!- CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD. CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: CC step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from CC riboflavin (ATP route): step 1/1. CC -!- SIMILARITY: Belongs to the RibF 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; L43967; AAC71363.1; -; Genomic_DNA. DR PIR; A64216; A64216. DR RefSeq; WP_009885831.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47391; -. DR STRING; 243273.MgenG_010200002084; -. DR EnsemblBacteria; AAC71363; AAC71363; MG_145. DR KEGG; mge:MG_145; -. DR PATRIC; 20009720; VBIMycGen98045_0166. DR eggNOG; ENOG4107WHP; Bacteria. DR eggNOG; COG0196; LUCA. DR KO; K11753; -. DR OrthoDB; EOG6QP0ZV; -. DR BioCyc; MGEN243273:GH2R-153-MONOMER; -. DR UniPathway; UPA00276; UER00406. DR UniPathway; UPA00277; UER00407. DR Proteomes; UP000000807; 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; IPR004821; Cyt_trans-like. 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; TIGR00125; cyt_tran_rel; 1. DR TIGRFAMs; TIGR00083; ribF; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; FAD; Flavoprotein; FMN; Kinase; KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 269 Putative riboflavin biosynthesis protein FT RibF. FT /FTId=PRO_0000194145. SQ SEQUENCE 269 AA; 31091 MW; A6F669F0450D03B0 CRC64; MKSLFIGYFD GLHQGHLFLK QNSKFEPMVL LIDNPPLKQT NWLYDLQQRV AQIKTYLKAT VEVFDVAKHN MNALSFFEQQ IKRLNCDEII VGTDWHFGND HKDGIWLKKL FKNTVIVNKT NLSSSVIRNY LTNNELEKAN QLLVEPYYRV GTVVHGLKKA RLLGFPTANI VMDNHLLTLN KGSYIVRVLL NNQTFYGIGF ISQKDQDLVC ETHIFNFNNE IYGSLVKFTL LKFIRTISKF SSQAALQKAI QSDANFALKW LENQNLDKI // ID RL11_MYCGE Reviewed; 137 AA. AC P47327; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 13-APR-2016, entry version 94. DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736}; GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; GN Synonyms=rpl11 {ECO:0000255|HAMAP-Rule:MF_00736}; GN OrderedLocusNames=MG081; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the CC ribosome interact with GTP-bound translation factors. CC {ECO:0000255|HAMAP-Rule:MF_00736}. 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 L12 dimers bind in a CC sequential fashion forming a multimeric L10(L12)X complex. CC {ECO:0000255|HAMAP-Rule:MF_00736}. 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; L43967; AAC71299.1; -; Genomic_DNA. DR PIR; I64208; I64208. DR RefSeq; WP_009885638.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47327; -. DR STRING; 243273.MgenG_010200000605; -. DR EnsemblBacteria; AAC71299; AAC71299; MG_081. DR KEGG; mge:MG_081; -. DR PATRIC; 20009564; VBIMycGen98045_0091. DR eggNOG; ENOG4108UIK; Bacteria. DR eggNOG; COG0080; LUCA. DR KO; K02867; -. DR OMA; QFEIEVG; -. DR OrthoDB; EOG69PQ9D; -. DR BioCyc; MGEN243273:GH2R-84-MONOMER; -. DR Proteomes; UP000000807; 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:0006412; P:translation; IEA:UniProtKB-HAMAP. 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 3: Inferred from homology; KW Complete proteome; Methylation; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 137 50S ribosomal protein L11. FT /FTId=PRO_0000104317. SQ SEQUENCE 137 AA; 14735 MW; A5DD5E6C4CD66E33 CRC64; MAKKTVTRIA KINLIGGQAK PGPALASVGI NMGEFTKQFN EKTKDRQGET IPCIITAFND KSFTFVLKTT PVSNLIKQAA KLEKGAKNAK TIVGKISLQQ AKEIAQYKLV DLNANTVEAA LKMVLGTAKQ MGIEVTD // ID RL15_MYCGE Reviewed; 150 AA. AC P47415; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=50S ribosomal protein L15 {ECO:0000255|HAMAP-Rule:MF_01341}; GN Name=rplO {ECO:0000255|HAMAP-Rule:MF_01341}; Synonyms=rpl15; GN OrderedLocusNames=MG169; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71387.1; -; Genomic_DNA. DR PIR; G64218; G64218. DR RefSeq; WP_010869361.1; NC_000908.2. DR ProteinModelPortal; P47415; -. DR EnsemblBacteria; AAC71387; AAC71387; MG_169. DR KEGG; mge:MG_169; -. DR PATRIC; 20009770; VBIMycGen98045_0191. DR KO; K02876; -. DR OMA; KRPLGAN; -. DR OrthoDB; EOG6CGCM5; -. DR BioCyc; MGEN243273:GH2R-178-MONOMER; -. DR Proteomes; UP000000807; 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: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; 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. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 150 50S ribosomal protein L15. FT /FTId=PRO_0000104758. SQ SEQUENCE 150 AA; 16501 MW; 08658548EB59E5FD CRC64; MELHQLKSVS KSRNHKSKVV GRGHGSGLGK TSSRGQKGQK ARKSGLTRLG FEGGQTPLYR RLPKYGVANK GILKKRWVVL NLNKVAKLNL KTVTRATLIE KKVISKKNNL PLKLIGNTKL TTPIHFEVQK ISKNALNAVQ TSKGSVKIIT // ID RIR1_MYCGE Reviewed; 721 AA. AC P47473; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase; GN Name=nrdE; OrderedLocusNames=MG231; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate + CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + CC thioredoxin. CC -!- ENZYME REGULATION: Under complex allosteric control mediated by CC deoxynucleoside triphosphates and ATP binding. The type of CC nucleotide bound at the specificity site determines substrate CC preference. It seems probable that ATP makes the enzyme reduce CDP CC and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction CC (By similarity). {ECO:0000250}. CC -!- PATHWAY: Genetic information processing; DNA replication. CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase CC large chain 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; L43967; AAC71452.1; -; Genomic_DNA. DR PIR; E64225; E64225. DR RefSeq; WP_009885768.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47473; -. DR SMR; P47473; 18-700. DR STRING; 243273.MgenG_010200001582; -. DR EnsemblBacteria; AAC71452; AAC71452; MG_231. DR KEGG; mge:MG_231; -. DR PATRIC; 20009944; VBIMycGen98045_0268. DR eggNOG; ENOG4105BZH; Bacteria. DR eggNOG; COG0209; LUCA. DR KO; K00525; -. DR OMA; DNMESIA; -. DR OrthoDB; EOG6J48HC; -. DR BioCyc; MGEN243273:GH2R-253-MONOMER; -. DR UniPathway; UPA00326; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. DR InterPro; IPR013346; NrdE_NrdA. DR InterPro; IPR026459; RNR_1b_NrdE. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. DR InterPro; IPR013554; RNR_N. DR InterPro; IPR008926; RNR_R1-su_N. DR Pfam; PF02867; Ribonuc_red_lgC; 1. DR Pfam; PF00317; Ribonuc_red_lgN; 1. DR Pfam; PF08343; RNR_N; 1. DR PRINTS; PR01183; RIBORDTASEM1. DR SUPFAM; SSF48168; SSF48168; 1. DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1. DR TIGRFAMs; TIGR04170; RNR_1b_NrdE; 1. DR PROSITE; PS00089; RIBORED_LARGE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Complete proteome; Disulfide bond; KW DNA replication; Nucleotide-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1 721 Ribonucleoside-diphosphate reductase FT subunit alpha. FT /FTId=PRO_0000187217. FT REGION 175 176 Substrate binding. {ECO:0000250}. FT REGION 384 388 Substrate binding. {ECO:0000250}. FT REGION 589 593 Substrate binding. {ECO:0000250}. FT ACT_SITE 384 384 Proton acceptor. {ECO:0000250}. FT ACT_SITE 386 386 Cysteine radical intermediate. FT {ECO:0000250}. FT ACT_SITE 388 388 Proton acceptor. {ECO:0000250}. FT BINDING 159 159 Substrate. {ECO:0000250}. FT BINDING 204 204 Substrate; via amide nitrogen. FT {ECO:0000250}. FT SITE 176 176 Important for hydrogen atom transfer. FT {ECO:0000250}. FT SITE 183 183 Allosteric effector binding. FT {ECO:0000250}. FT SITE 213 213 Allosteric effector binding. FT {ECO:0000250}. FT SITE 413 413 Important for hydrogen atom transfer. FT {ECO:0000250}. FT SITE 694 694 Important for electron transfer. FT {ECO:0000250}. FT SITE 695 695 Important for electron transfer. FT {ECO:0000250}. FT SITE 716 716 Interacts with thioredoxin/glutaredoxin. FT {ECO:0000250}. FT SITE 719 719 Interacts with thioredoxin/glutaredoxin. FT {ECO:0000250}. FT DISULFID 176 413 Redox-active. {ECO:0000250}. SQ SEQUENCE 721 AA; 82249 MW; 75E0174979CCAA59 CRC64; MTSKEKIPTF NTEEDVESYI SFNAQAKIYD DFAIDLQAVE SYIQEHVKPK TKVFHSTKER LDFLIKNDYY DEKIINMYSF EQFEEITHKA YSYRFRYANF MGAFKFYNAY ALKTFDGKYY LENYEDRVVM NVLMLANGNF NKALKLLKQI ILNRFQPATP TFLNAGRKKR GEFVSCYLLR IEDNMESIGR AITTTLQLSK RDGGVALLLS NLREAGAPIK KIENQSSGII PIMKLLEDSF SYSNQLGQRQ GAGAVYLHCH HPDVMQFLDT KRENADEKIR IKSLSLGLVI PDITFQLAKN NEMMALFSPY DIYQEYGKAL SDISVTEMYY ELLENQRIKK TFISARKFFQ TIAELHFESG YPYILFDDTV NRRNAHKNRI VMSNLCSEIV QPSLPSEFYS DLTFKKVGSD ISCNLGSLNI ARAMESGSEL AELIQLAIES LDLVSRISSL ETAPSIKKGN SENHALGLGA MNLHGFLATN AIYYDSKEAV DFTNIFFYTV AYHAFSASNK LALELGKFKD FENTKFADGS YFDKYTKVAS DFWTCKTEKV QALFDKYQVK IPTQENWKQL VASIQKDGLA NSHLMAIAPT GSISYLSSCT PSLQPVVSPV EVRKEGKLGR IYVPAYKLDN DNYQYFKDGA YELGFEPIIN IVAAAQQHVD QAISLTLFMT DKATTRDLNK AYIYAFKKGC SSIYYVRVRQ DVLKDSEDHT IKIKDCEVCS I // ID RIR2_MYCGE Reviewed; 340 AA. AC P47471; Q49443; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase small subunit; GN Name=nrdF; OrderedLocusNames=MG229; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 234-340. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate + CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + CC thioredoxin. CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 2 iron ions per subunit. {ECO:0000250}; CC -!- PATHWAY: Genetic information processing; DNA replication. CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase CC small chain family. {ECO:0000305}. CC -!- CAUTION: Seems to lack two of the iron-binding residues. 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; L43967; AAC71450.1; -; Genomic_DNA. DR EMBL; U01739; AAD10549.1; -; Genomic_DNA. DR PIR; C64225; C64225. DR ProteinModelPortal; P47471; -. DR SMR; P47471; 18-308. DR STRING; 243273.MgenG_010200001572; -. DR EnsemblBacteria; AAC71450; AAC71450; MG_229. DR KEGG; mge:MG_229; -. DR PATRIC; 20009940; VBIMycGen98045_0266. DR eggNOG; ENOG4107R25; Bacteria. DR eggNOG; COG0208; LUCA. DR KO; K00526; -. DR OMA; YYQADEP; -. DR OrthoDB; EOG68DD19; -. DR BioCyc; MGEN243273:GH2R-251-MONOMER; -. DR UniPathway; UPA00326; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC. DR GO; GO:0009186; P:deoxyribonucleoside diphosphate metabolic process; IEA:InterPro. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.620.20; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012348; RNR-rel. DR InterPro; IPR026494; RNR_NrdF. DR InterPro; IPR000358; RNR_small. DR PANTHER; PTHR23409; PTHR23409; 1. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR TIGRFAMs; TIGR04171; RNR_1b_NrdF; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; Iron; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 340 Ribonucleoside-diphosphate reductase FT subunit beta. FT /FTId=PRO_0000190483. FT ACT_SITE 126 126 {ECO:0000250}. FT METAL 88 88 Iron 1. {ECO:0000250}. FT METAL 122 122 Iron 1. {ECO:0000250}. FT METAL 216 216 Iron 2. FT CONFLICT 234 243 AKQKEMKAFV -> SKTKGDESIC (in Ref. 2; FT AAD10549). {ECO:0000305}. SQ SEQUENCE 340 AA; 39152 MW; F0ED1BDAFB2B9CFD CRC64; MAANNKKYFL ESFSPLGYVK NNFQGNLRSV NWNLVDDEKD LEVWNRIVQN FWLPEKIPVS NDIPSWKKLS KDWQDLITKT FTGLTLLDTI QATIGDICQI DHALTDHEQV IYANFAFMVG VHARSYGTIF STLCTSEQIN AAHEWVVNTE SLQKRAKALI PYYTGNDPLK SKVAAALMPG FLLYGGFYLP FYLSSRKQLP NTSDIIRLIL RDKVIHNYYS GYKYQRKLEK LPLAKQKEMK AFVFELMYRL IELEKDYLKE LYEGFGIVDD AIKFSVYNAG KFLQNLGYDS PFTAAETRIK PEIFAQLSAR ADENHDFFSG NGSSYVMGVS EETNDDDWNF // ID RL19_MYCGE Reviewed; 119 AA. AC P47682; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 84. DE RecName: Full=50S ribosomal protein L19; GN Name=rplS; Synonyms=rpl19; OrderedLocusNames=MG444; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC72464.1; -; Genomic_DNA. DR PIR; A64249; A64249. DR RefSeq; WP_010869484.1; NC_000908.2. DR ProteinModelPortal; P47682; -. DR STRING; 243273.MgenG_010200000230; -. DR EnsemblBacteria; AAC72464; AAC72464; MG_444. DR KEGG; mge:MG_444; -. DR PATRIC; 20010476; VBIMycGen98045_0511. DR eggNOG; COG0335; LUCA. DR KO; K02884; -. DR OMA; TFTIRKM; -. DR OrthoDB; EOG6DZF5W; -. DR BioCyc; MGEN243273:GH2R-497-MONOMER; -. DR Proteomes; UP000000807; 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_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 1 119 50S ribosomal protein L19. FT /FTId=PRO_0000163485. SQ SEQUENCE 119 AA; 13846 MW; 5C2349D8DFA67869 CRC64; MKKINKQALI DAVEQKQLKE YVPEFGAGDE VNVAIKLREK EKVRVQNFTG TVLRRRGRGI SETFMVRKTT DGIPIEKNFQ IHNPNIDIEV KRRGKVRRAY ISYMRERSGK SAKIKEKKS // ID RL1_MYCGE Reviewed; 226 AA. AC P47328; Q59520; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318}; GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; GN Synonyms=rpl1 {ECO:0000255|HAMAP-Rule:MF_01318}; GN OrderedLocusNames=MG082; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71300.1; -; Genomic_DNA. DR EMBL; U02113; AAD12387.1; ALT_SEQ; Genomic_DNA. DR PIR; A64209; A64209. DR RefSeq; WP_010869323.1; NC_000908.2. DR ProteinModelPortal; P47328; -. DR STRING; 243273.MgenG_010200000620; -. DR EnsemblBacteria; AAC71300; AAC71300; MG_082. DR KEGG; mge:MG_082; -. DR PATRIC; 20009566; VBIMycGen98045_0092. DR eggNOG; ENOG4105C64; Bacteria. DR eggNOG; COG0081; LUCA. DR KO; K02863; -. DR OMA; NEGWTDF; -. DR OrthoDB; EOG6FBX2G; -. DR BioCyc; MGEN243273:GH2R-85-MONOMER; -. DR Proteomes; UP000000807; 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 1 226 50S ribosomal protein L1. FT /FTId=PRO_0000125687. SQ SEQUENCE 226 AA; 24685 MW; 710C0921FB8BCEF8 CRC64; MKKLSKRMQA VTKLIDKNKL YPIQEAFELI KKTAITKFVS SVDIAVSLNL DTTKAEQQLR GAIAFPFSIG KSIRILAITD DEKKASEAGA DFVGGLDKIE AIKNGWLDFD LIITSPKFMG ALGKLGKLLG TRGLMPNPKT ETVTDDVVSA IKAYKKGKKE YRTDSFGNIH LSLGKTDTKT EHLVANAMAL IDLIKSKRPS TVKGTYIKNI ALTTTMGPSL KVKLPD // ID RL23_MYCGE Reviewed; 106 AA. AC P47399; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369}; GN Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369}; GN Synonyms=rpl23 {ECO:0000255|HAMAP-Rule:MF_01369}; GN OrderedLocusNames=MG153; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71371.1; -; Genomic_DNA. DR PIR; I64216; I64216. DR RefSeq; WP_009885837.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47399; -. DR STRING; 243273.MgenG_010200002154; -. DR EnsemblBacteria; AAC71371; AAC71371; MG_153. DR KEGG; mge:MG_153; -. DR PATRIC; 20009738; VBIMycGen98045_0175. DR eggNOG; ENOG4108B8U; Bacteria. DR eggNOG; COG0089; LUCA. DR KO; K02892; -. DR OrthoDB; EOG6HTP4P; -. DR BioCyc; MGEN243273:GH2R-162-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. 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; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. 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; IPR013025; Ribosomal_L25/23. DR Pfam; PF00276; Ribosomal_L23; 1. DR SUPFAM; SSF54189; SSF54189; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 106 50S ribosomal protein L23. FT /FTId=PRO_0000129418. SQ SEQUENCE 106 AA; 11880 MW; 4F88C14C3990E679 CRC64; MDVTNILLKP VLTEKSYLNQ MGELKKYVFA INPKATKTKV KLAFEIIYGV KPLKINTLIR KPVTIRNGTK YPGFSKLAKL AVITLPKGMD IAITGEKTTK KETKDQ // ID RL14_MYCGE Reviewed; 122 AA. AC P47407; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367}; GN Name=rplN {ECO:0000255|HAMAP-Rule:MF_01367}; GN Synonyms=rpl14 {ECO:0000255|HAMAP-Rule:MF_01367}; GN OrderedLocusNames=MG161; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71379.1; -; Genomic_DNA. DR PIR; H64217; H64217. DR RefSeq; WP_009885845.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47407; -. DR SMR; P47407; 1-122. DR STRING; 243273.MgenG_010200002194; -. DR EnsemblBacteria; AAC71379; AAC71379; MG_161. DR KEGG; mge:MG_161; -. DR PATRIC; 20009754; VBIMycGen98045_0183. DR eggNOG; ENOG4108UNN; Bacteria. DR eggNOG; COG0093; LUCA. DR KO; K02874; -. DR OMA; LRDKQFM; -. DR OrthoDB; EOG6GBMJ6; -. DR BioCyc; MGEN243273:GH2R-170-MONOMER; -. DR Proteomes; UP000000807; 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: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_0000128551. SQ SEQUENCE 122 AA; 13466 MW; 91D8B78B7E5A032F CRC64; MVSFMTRLNV ADNTGAKQVG IIKVLGATYK RYAFLGDVVV VSVKDAIPNG MVKKGQVLRA VIVRTKKGQQ RQDGTHLKFH DNACVLIKED KSPRGTRIFG PVARELREKG YNKILSLAVE VV // ID RL16_MYCGE Reviewed; 138 AA. AC P47404; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=50S ribosomal protein L16 {ECO:0000255|HAMAP-Rule:MF_01342}; GN Name=rplP {ECO:0000255|HAMAP-Rule:MF_01342}; GN Synonyms=rpl16 {ECO:0000255|HAMAP-Rule:MF_01342}; GN OrderedLocusNames=MG158; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71376.1; -; Genomic_DNA. DR PIR; E64217; E64217. DR RefSeq; WP_009885842.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47404; -. DR STRING; 243273.MgenG_010200002179; -. DR EnsemblBacteria; AAC71376; AAC71376; MG_158. DR KEGG; mge:MG_158; -. DR PATRIC; 20009748; VBIMycGen98045_0180. DR eggNOG; ENOG4108R70; Bacteria. DR eggNOG; COG0197; LUCA. DR KO; K02878; -. DR OMA; KGAVEYW; -. DR OrthoDB; EOG6WHNWS; -. DR BioCyc; MGEN243273:GH2R-167-MONOMER; -. DR Proteomes; UP000000807; 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: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 1 138 50S ribosomal protein L16. FT /FTId=PRO_0000062141. SQ SEQUENCE 138 AA; 15615 MW; 874CB142B5AECDED CRC64; MLQPKRTKYR KPHNVSYEGH TKGNGYVAFG EYGIVATKGN WIDARAIESA RVAISKCLGK TGKMWIRIFP HMSKTKKPLE VRMGSGKGNP EFWVAVVKKG TVMFEVANIP EQQMIKALTR AGHKLPVTWK LMKREENS // ID RL22_MYCGE Reviewed; 144 AA. AC P47402; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 85. DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331}; GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; GN Synonyms=rpl22 {ECO:0000255|HAMAP-Rule:MF_01331}; GN OrderedLocusNames=MG156; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71374.1; -; Genomic_DNA. DR PIR; C64217; C64217. DR RefSeq; WP_009885840.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47402; -. DR STRING; 243273.MgenG_010200002169; -. DR EnsemblBacteria; AAC71374; AAC71374; MG_156. DR KEGG; mge:MG_156; -. DR PATRIC; 20009744; VBIMycGen98045_0178. DR eggNOG; ENOG4105KAP; Bacteria. DR eggNOG; COG0091; LUCA. DR KO; K02890; -. DR OMA; MGKSANP; -. DR OrthoDB; EOG6V4GKB; -. DR BioCyc; MGEN243273:GH2R-165-MONOMER; -. DR Proteomes; UP000000807; 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: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 1 144 50S ribosomal protein L22. FT /FTId=PRO_0000125177. SQ SEQUENCE 144 AA; 16131 MW; 96ADCE6FDCE15D43 CRC64; MIAFAKQYRV HISPQKARLV CQLIVGKKIN DAQNILLNTP KKAAYFLTKL LNSAISNATN NHGMSGDLLY VFECVANQGP SMKRTIARAK GSGSVLTKRS SNLVIKLSDN PNERKLLLTQ QKELVKKRTM GHKKEKAKQK QKQQ // ID RL10_MYCGE Reviewed; 162 AA. AC P36263; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 13-APR-2016, entry version 92. DE RecName: Full=50S ribosomal protein L10; GN Name=rplJ; Synonyms=rpl10; OrderedLocusNames=MG361; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 92-162. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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. {ECO:0000250}. CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. CC The N-terminus interacts with L11 and the large rRNA to form the CC base of the stalk. The C-terminus forms an elongated spine to CC which L12 dimers bind in a sequential fashion forming a multimeric CC L10(L12)X complex (By similarity). {ECO:0000250}. 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; L43967; AAC71587.1; -; Genomic_DNA. DR EMBL; U02206; AAD12496.1; -; Genomic_DNA. DR PIR; I64239; I64239. DR RefSeq; WP_009885818.1; NZ_AAGX01000006.1. DR ProteinModelPortal; P36263; -. DR STRING; 243273.MgenG_010200001958; -. DR EnsemblBacteria; AAC71587; AAC71587; MG_361. DR KEGG; mge:MG_361; -. DR PATRIC; 20010302; VBIMycGen98045_0425. DR eggNOG; ENOG4107URM; Bacteria. DR eggNOG; COG0244; LUCA. DR KO; K02864; -. DR OMA; VWGTEDE; -. DR OrthoDB; EOG6DNTDR; -. DR BioCyc; MGEN243273:GH2R-415-MONOMER; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 162 50S ribosomal protein L10. FT /FTId=PRO_0000154665. SQ SEQUENCE 162 AA; 18261 MW; AC4CC72724389AEC CRC64; MVDSKKNKKQ QVTDFSNLLS QSKGFVIFDY SGMSAVDATL MRKKLFNKGS KIKIVKNNIL RRALKTSNFE GVDESVIKGK IAVAVGINEI LETLKVVDSV VKEKELMKFV CGHFDNRIFN SDDLQKIAKL PGRNELYGMF LSVLQAPLRK FLYALQAVRN AK // ID RL21_MYCGE Reviewed; 100 AA. AC P47474; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=50S ribosomal protein L21 {ECO:0000255|HAMAP-Rule:MF_01363}; GN Name=rplU {ECO:0000255|HAMAP-Rule:MF_01363}; GN Synonyms=rpl21 {ECO:0000255|HAMAP-Rule:MF_01363}; GN OrderedLocusNames=MG232; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71453.1; -; Genomic_DNA. DR EMBL; U02141; AAD12418.1; -; Genomic_DNA. DR PIR; F64225; F64225. DR RefSeq; WP_009885769.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47474; -. DR STRING; 243273.MgenG_010200001587; -. DR EnsemblBacteria; AAC71453; AAC71453; MG_232. DR KEGG; mge:MG_232; -. DR PATRIC; 20009946; VBIMycGen98045_0269. DR eggNOG; ENOG4107Y7S; Bacteria. DR eggNOG; COG0261; LUCA. DR KO; K02888; -. DR OrthoDB; EOG6TJ84X; -. DR BioCyc; MGEN243273:GH2R-254-MONOMER; -. DR Proteomes; UP000000807; 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_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 1 100 50S ribosomal protein L21. FT /FTId=PRO_0000181006. SQ SEQUENCE 100 AA; 11606 MW; CAAAE6F21B208FBD CRC64; MHAIVVCGAK QYLVHENESI FVEKLAGKVG QEIQLDKVLM LDEKIGKPYL EKAKVVCVIE KHGLKSKIKL IKHISQKHHL KRYGHRQPYT KLKVVRFIHD // ID RL27_MYCGE Reviewed; 104 AA. AC P47476; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=50S ribosomal protein L27 {ECO:0000255|HAMAP-Rule:MF_00539}; GN Name=rpmA {ECO:0000255|HAMAP-Rule:MF_00539}; GN Synonyms=rpl27 {ECO:0000255|HAMAP-Rule:MF_00539}; GN OrderedLocusNames=MG234; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the ribosomal protein L27P family. CC {ECO:0000255|HAMAP-Rule:MF_00539}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71455.1; -; Genomic_DNA. DR PIR; H64225; H64225. DR RefSeq; WP_009885771.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47476; -. DR SMR; P47476; 16-87. DR STRING; 243273.MgenG_010200001597; -. DR EnsemblBacteria; AAC71455; AAC71455; MG_234. DR KEGG; mge:MG_234; -. DR PATRIC; 20009950; VBIMycGen98045_0271. DR eggNOG; ENOG4105K46; Bacteria. DR eggNOG; COG0211; LUCA. DR KO; K02899; -. DR OMA; LIMNLQL; -. DR OrthoDB; EOG6N94H6; -. DR BioCyc; MGEN243273:GH2R-256-MONOMER; -. DR Proteomes; UP000000807; 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_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 1 104 50S ribosomal protein L27. FT /FTId=PRO_0000181121. SQ SEQUENCE 104 AA; 11572 MW; 31C377704191C323 CRC64; MSKNSYCYQI NLQFFASKKG VGSTKNGRDS HSKRLGAKKA DGQMIRVGQI IYRQRGTKIF AGQNVAMGSD NTLFALSDGI VRFQKFGSKQ SKTRVNIIKH QLNA // ID RL32_MYCGE Reviewed; 57 AA. AC P47603; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 13-APR-2016, entry version 81. DE RecName: Full=50S ribosomal protein L32; GN Name=rpmF; Synonyms=rpl32; OrderedLocusNames=MG363; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71589.1; -; Genomic_DNA. DR PIR; B64240; B64240. DR ProteinModelPortal; P47603; -. DR STRING; 243273.MgenG_010200001968; -. DR EnsemblBacteria; AAC71589; AAC71589; MG_363. DR KEGG; mge:MG_363; -. DR PATRIC; 20010306; VBIMycGen98045_0427. DR eggNOG; COG0333; LUCA. DR KO; K02911; -. DR OMA; CSCGMYG; -. DR OrthoDB; EOG6VMTT4; -. DR BioCyc; MGEN243273:GH2R-417-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. 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 57 50S ribosomal protein L32. FT /FTId=PRO_0000172365. SQ SEQUENCE 57 AA; 6623 MW; F9B1C7231FC4287D CRC64; MAVQQRRSSK HRRDKRRSHD ALTLQTLSVC KKCGKKKLSH RVCSCGMYGE LRVKKAH // ID RL13_MYCGE Reviewed; 146 AA. AC P47657; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=50S ribosomal protein L13 {ECO:0000255|HAMAP-Rule:MF_01366}; GN Name=rplM {ECO:0000255|HAMAP-Rule:MF_01366}; GN Synonyms=rpl13 {ECO:0000255|HAMAP-Rule:MF_01366}; GN OrderedLocusNames=MG418; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-146. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71644.1; -; Genomic_DNA. DR EMBL; U01744; AAD10555.1; -; Genomic_DNA. DR PIR; B64246; B64246. DR RefSeq; WP_010869476.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47657; -. DR STRING; 243273.MgenG_010200000395; -. DR EnsemblBacteria; AAC71644; AAC71644; MG_418. DR KEGG; mge:MG_418; -. DR PATRIC; 20010424; VBIMycGen98045_0485. DR eggNOG; ENOG4108UM5; Bacteria. DR eggNOG; COG0102; LUCA. DR KO; K02871; -. DR OMA; YTPHMDC; -. DR OrthoDB; EOG628FBD; -. DR BioCyc; MGEN243273:GH2R-473-MONOMER; -. DR Proteomes; UP000000807; 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; 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 1 146 50S ribosomal protein L13. FT /FTId=PRO_0000133741. SQ SEQUENCE 146 AA; 16667 MW; D2F19B15FA96567A CRC64; MQKTSMLTKE EAIKNRKWYL VDASGLVLGK LAVKAANLIR GKNKANFTPN QDCGDHLIII NSDQVVLTGN KKDNEFWYHH SQYMGGIKKT SGRDMINKNS DKLVFNAVKG MLPDNRLSRR LITKVHVFKN DKHNMEAQKP TLLNWS // ID RL17_MYCGE Reviewed; 123 AA. AC P47424; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=50S ribosomal protein L17 {ECO:0000255|HAMAP-Rule:MF_01368}; GN Name=rplQ {ECO:0000255|HAMAP-Rule:MF_01368}; GN Synonyms=rpl17 {ECO:0000255|HAMAP-Rule:MF_01368}; GN OrderedLocusNames=MG178; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71397.1; -; Genomic_DNA. DR PIR; G64219; G64219. DR RefSeq; WP_010869362.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47424; -. DR STRING; 243273.MgenG_010200002294; -. DR EnsemblBacteria; AAC71397; AAC71397; MG_178. DR KEGG; mge:MG_178; -. DR PATRIC; 20009788; VBIMycGen98045_0200. DR eggNOG; ENOG4108ZT0; Bacteria. DR eggNOG; COG0203; LUCA. DR KO; K02879; -. DR OMA; MGDATEM; -. DR OrthoDB; EOG6GR3GR; -. DR BioCyc; MGEN243273:GH2R-187-MONOMER; -. DR Proteomes; UP000000807; 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; 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. DR PROSITE; PS01167; RIBOSOMAL_L17; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 123 50S ribosomal protein L17. FT /FTId=PRO_0000175533. SQ SEQUENCE 123 AA; 14107 MW; 8FC8B15FA86336A7 CRC64; MSYINKEGKT TAWRVMTVRQ QVSAVLSYGK IQTTLKKAKN TQKRLEKIIT IAKVDNFNNR RAVKKWLLNT NSLDVDQLTN HLFKKVAPRF LKRNGGYSRV LKLGVRRGDS TEMAILQLID ATN // ID RL24_MYCGE Reviewed; 108 AA. AC P47408; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326}; GN Name=rplX {ECO:0000255|HAMAP-Rule:MF_01326}; GN Synonyms=rpl24 {ECO:0000255|HAMAP-Rule:MF_01326}; GN OrderedLocusNames=MG162; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71380.1; -; Genomic_DNA. DR PIR; I64217; I64217. DR RefSeq; WP_009885846.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47408; -. DR STRING; 243273.MgenG_010200002199; -. DR EnsemblBacteria; AAC71380; AAC71380; MG_162. DR KEGG; mge:MG_162; -. DR PATRIC; 20009756; VBIMycGen98045_0184. DR eggNOG; ENOG41080DU; Bacteria. DR eggNOG; COG0198; LUCA. DR KO; K02895; -. DR OrthoDB; EOG6FFSDM; -. DR BioCyc; MGEN243273:GH2R-171-MONOMER; -. DR Proteomes; UP000000807; 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; 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; 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 1 108 50S ribosomal protein L24. FT /FTId=PRO_0000130678. SQ SEQUENCE 108 AA; 12132 MW; 1CE6714EE1E0E29F CRC64; MQRIRKGDKV VVITGKNKGG SGIVLKVLTK QNKAIVEGIN KVTVHKKEQV NKRSKQTNPT TKEAPLPLNK LALFDQKAKQ QTIGKIKYQI DPKTKQKTRV FKKTNNAI // ID RL29_MYCGE Reviewed; 200 AA. AC P47405; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=50S ribosomal protein L29; GN Name=rpmC; Synonyms=rpl29; OrderedLocusNames=MG159; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71377.1; -; Genomic_DNA. DR PIR; F64217; F64217. DR RefSeq; WP_009885843.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47405; -. DR STRING; 243273.MgenG_010200002184; -. DR EnsemblBacteria; AAC71377; AAC71377; MG_159. DR KEGG; mge:MG_159; -. DR PATRIC; 20009750; VBIMycGen98045_0181. DR eggNOG; COG0255; LUCA. DR KO; K02904; -. DR OMA; LIVNSWK; -. DR OrthoDB; EOG6VTK8Z; -. DR BioCyc; MGEN243273:GH2R-168-MONOMER; -. DR Proteomes; UP000000807; 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:InterPro. 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 200 50S ribosomal protein L29. FT /FTId=PRO_0000130420. FT REGION 1 77 50S ribosomal protein L29. FT REGION 78 200 Unknown. SQ SEQUENCE 200 AA; 23258 MW; 5BC115E52AA5EA92 CRC64; MTIAKELKQK SNEELVKLVI KLKGELLEYR FKLAHGELDK PHLIAKVRKL LAVVLTILTE RKLNWQVEKD KYKLLSRKTN ELIVNSWKQK LSTKPESKQE TKKAEVKPKV ESKPESKQET KKAEVKPLKQ ETKKVEVKPK VEPKPLKQET KKVEARIETK TKVESKPLKQ EVKKVEAKKS VSKPQKPVKA KMIKTKEKKQ // ID RL36_MYCGE Reviewed; 37 AA. AC P47420; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=50S ribosomal protein L36 {ECO:0000255|HAMAP-Rule:MF_00251}; GN Name=rpmJ {ECO:0000255|HAMAP-Rule:MF_00251}; Synonyms=rpl36; GN OrderedLocusNames=MG174; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71393.1; -; Genomic_DNA. DR PIR; C64219; C64219. DR RefSeq; WP_009885859.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47420; -. DR SMR; P47420; 1-37. DR STRING; 243273.MgenG_010200002274; -. DR EnsemblBacteria; AAC71393; AAC71393; MG_174. DR KEGG; mge:MG_174; -. DR PATRIC; 20009780; VBIMycGen98045_0196. DR eggNOG; ENOG41067V7; Bacteria. DR eggNOG; COG0257; LUCA. DR KO; K02919; -. DR OrthoDB; EOG676ZC2; -. DR BioCyc; MGEN243273:GH2R-183-MONOMER; -. DR Proteomes; UP000000807; 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 37 50S ribosomal protein L36. FT /FTId=PRO_0000126214. SQ SEQUENCE 37 AA; 4429 MW; CD817B0CC6B19FC3 CRC64; MKVRASVKPI CKDCKIIKRH RILRVICKTK KHKQRQG // ID RL18_MYCGE Reviewed; 115 AA. AC P47413; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=50S ribosomal protein L18 {ECO:0000255|HAMAP-Rule:MF_01337}; GN Name=rplR {ECO:0000255|HAMAP-Rule:MF_01337}; GN Synonyms=rpl18 {ECO:0000255|HAMAP-Rule:MF_01337}; GN OrderedLocusNames=MG167; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71385.1; -; Genomic_DNA. DR PIR; E64218; E64218. DR RefSeq; WP_009885853.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47413; -. DR STRING; 243273.MgenG_010200002234; -. DR EnsemblBacteria; AAC71385; AAC71385; MG_167. DR KEGG; mge:MG_167; -. DR PATRIC; 20009766; VBIMycGen98045_0189. DR eggNOG; ENOG4105K4C; Bacteria. DR eggNOG; COG0256; LUCA. DR KO; K02881; -. DR OMA; NEFIFDR; -. DR OrthoDB; EOG64NB48; -. DR BioCyc; MGEN243273:GH2R-176-MONOMER; -. DR Proteomes; UP000000807; 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_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 1 115 50S ribosomal protein L18. FT /FTId=PRO_0000131295. SQ SEQUENCE 115 AA; 12926 MW; 749F62ED1EE2D631 CRC64; MTRNDKRRIR HKRIVKKIRL TNLNNRVVLI VIKSLKNISV QAWDFSKNVV LTSSSSLQLK LKNGNKENAK LVGMDIATKL IKLNQKDVVF DTGGSKYHGR IAALAEGARA KGLNF // ID RL20_MYCGE Reviewed; 124 AA. AC P47440; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=50S ribosomal protein L20; GN Name=rplT; Synonyms=rpl20; OrderedLocusNames=MG198; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71416.1; -; Genomic_DNA. DR PIR; H64221; H64221. DR RefSeq; WP_009885739.1; NZ_AAGX01000004.1. DR ProteinModelPortal; P47440; -. DR STRING; 243273.MgenG_010200001322; -. DR EnsemblBacteria; AAC71416; AAC71416; MG_198. DR KEGG; mge:MG_198; -. DR PATRIC; 20009848; VBIMycGen98045_0230. DR eggNOG; ENOG4108YZX; Bacteria. DR eggNOG; COG0292; LUCA. DR KO; K02887; -. DR OMA; RKAKEQM; -. DR OrthoDB; EOG6CGCMB; -. DR BioCyc; MGEN243273:GH2R-206-MONOMER; -. DR Proteomes; UP000000807; 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:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-HAMAP. 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 1 124 50S ribosomal protein L20. FT /FTId=PRO_0000177181. SQ SEQUENCE 124 AA; 14361 MW; 54DEC5FB524BBC89 CRC64; MRVKGTNTTR IRRKKWLKQA SGSFGTRKAS FKAAKQTVIQ ASKYAYRDRR QKKREFRSLW ILRLNAALRA QGMTYSVFIN ELKKAKIVIN RKVLSELAIK EPNKLNLIIN TIKKPTNKPT VAKT // ID RL331_MYCGE Reviewed; 53 AA. AC P47567; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 84. DE RecName: Full=50S ribosomal protein L33 1; GN Name=rpmG1; Synonyms=rpl33, rpmG; OrderedLocusNames=MG325; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71547.1; -; Genomic_DNA. DR PIR; I64235; I64235. DR RefSeq; WP_009885961.1; NC_000908.2. DR ProteinModelPortal; P47567; -. DR STRING; 243273.MgenG_010200003063; -. DR EnsemblBacteria; AAC71547; AAC71547; MG_325. DR KEGG; mge:MG_325; -. DR PATRIC; 20010206; VBIMycGen98045_0380. DR eggNOG; ENOG4108C4V; Bacteria. DR eggNOG; COG0267; LUCA. DR KO; K02913; -. DR OMA; STRLGCN; -. DR OrthoDB; EOG60KNBM; -. DR BioCyc; MGEN243273:GH2R-373-MONOMER; -. DR Proteomes; UP000000807; 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_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 53 50S ribosomal protein L33 1. FT /FTId=PRO_0000170187. SQ SEQUENCE 53 AA; 6240 MW; D05E4DD01CBAF7D4 CRC64; MAVKRSTRLG CNECSEINYL TFKNVKKNPE KLALNKFCSR CRKVVLHKEV KRK // ID RL332_MYCGE Reviewed; 48 AA. AC Q9ZB82; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=50S ribosomal protein L33 2; GN Name=rpmG2; OrderedLocusNames=MG055.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. 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; L43967; AAC71272.1; -; Genomic_DNA. DR ProteinModelPortal; Q9ZB82; -. DR STRING; 243273.MgenG_010200001160; -. DR EnsemblBacteria; AAC71272; AAC71272; MG_473. DR KEGG; mge:MG_473; -. DR eggNOG; COG0267; LUCA. DR KO; K02913; -. DR OrthoDB; EOG60KNBM; -. DR BioCyc; MGEN243273:GH2R-56-MONOMER; -. DR Proteomes; UP000000807; 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_00294; Ribosomal_L33; 1. DR InterPro; IPR001705; Ribosomal_L33. DR InterPro; IPR011332; Ribosomal_zn-bd. DR Pfam; PF00471; Ribosomal_L33; 1. DR SUPFAM; SSF57829; SSF57829; 1. DR TIGRFAMs; TIGR01023; rpmG_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 48 50S ribosomal protein L33 2. FT /FTId=PRO_0000170188. SQ SEQUENCE 48 AA; 5946 MW; 33C7A47A3B98B65F CRC64; MRKKIIFVCQ DCLSRNYVKR WTKQPLQRLI INKYCKQCNQ KTKHLDSF // ID RL35_MYCGE Reviewed; 59 AA. AC P47439; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=50S ribosomal protein L35 {ECO:0000255|HAMAP-Rule:MF_00514}; GN Name=rpmI {ECO:0000255|HAMAP-Rule:MF_00514}; GN Synonyms=rpl35 {ECO:0000255|HAMAP-Rule:MF_00514}; GN OrderedLocusNames=MG197; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71415.1; -; Genomic_DNA. DR PIR; G64221; G64221. DR RefSeq; WP_009885738.1; NZ_AAGX01000004.1. DR ProteinModelPortal; P47439; -. DR STRING; 243273.MgenG_010200001317; -. DR EnsemblBacteria; AAC71415; AAC71415; MG_197. DR KEGG; mge:MG_197; -. DR PATRIC; 20009846; VBIMycGen98045_0229. DR eggNOG; ENOG41086CC; Bacteria. DR eggNOG; COG0291; LUCA. DR KO; K02916; -. DR OMA; KQKRHAR; -. DR OrthoDB; EOG651T3B; -. DR BioCyc; MGEN243273:GH2R-205-MONOMER; -. DR Proteomes; UP000000807; 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 59 50S ribosomal protein L35. FT /FTId=PRO_0000177381. SQ SEQUENCE 59 AA; 6766 MW; B02D7794F65F444E CRC64; MKTKSAAVKR FKLTKSGQIK RKHAYTSHLA PHKSTKQKRH LRKQATVSNS ELKRIGILI // ID RL3_MYCGE Reviewed; 257 AA. AC P47397; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 84. DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325}; GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; GN Synonyms=rpl3 {ECO:0000255|HAMAP-Rule:MF_01325}; GN OrderedLocusNames=MG151; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-176. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71369.1; -; Genomic_DNA. DR EMBL; U02153; AAD12434.1; -; Genomic_DNA. DR PIR; G64216; G64216. DR RefSeq; WP_010869358.1; NC_000908.2. DR ProteinModelPortal; P47397; -. DR EnsemblBacteria; AAC71369; AAC71369; MG_151. DR KEGG; mge:MG_151; -. DR PATRIC; 20009734; VBIMycGen98045_0173. DR KO; K02906; -. DR OMA; QVWDENN; -. DR OrthoDB; EOG6WDSMH; -. DR BioCyc; MGEN243273:GH2R-160-MONOMER; -. DR Proteomes; UP000000807; 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 1 257 50S ribosomal protein L3. FT /FTId=PRO_0000077120. SQ SEQUENCE 257 AA; 28488 MW; C3ECBEE824CB4E3E CRC64; MDVRGIFGVK VGMSQIFTEQ NECLPITIVY CEANQVAGIK TIAKDNYNAT LLSFQTVDEK QLNKPKQGFF SKLKLEPHKY LREIRKMQGF ELGKKITPQE LFKIGEYVDV TSLTKGRGFT GAIKRWNFKI GPLGHGAGYP HRFQGSVQAG RGGSSAQRVF KGKKMSGHYG HEQVTIQNLF IVGFDEINKL VLVSGAIAGP EGGIVLIKTA KKKTGKIKDI KLAVQTVKAP QLKAPKKQKT KVETNQVNPK IEEEKTK // ID RL31_MYCGE Reviewed; 97 AA. AC P47499; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501}; GN Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501}; GN Synonyms=rpl31 {ECO:0000255|HAMAP-Rule:MF_00501}; GN OrderedLocusNames=MG257; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Binds the 23S rRNA. {ECO:0000255|HAMAP-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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71477.1; -; Genomic_DNA. DR PIR; D64228; D64228. DR RefSeq; WP_010869398.1; NC_000908.2. DR ProteinModelPortal; P47499; -. DR STRING; 243273.MgenG_010200001772; -. DR EnsemblBacteria; AAC71477; AAC71477; MG_257. DR KEGG; mge:MG_257; -. DR PATRIC; 20010002; VBIMycGen98045_0294. DR eggNOG; ENOG41082EV; Bacteria. DR eggNOG; COG0254; LUCA. DR KO; K02909; -. DR OMA; TVNIDIC; -. DR OrthoDB; EOG6DVJZM; -. DR BioCyc; MGEN243273:GH2R-282-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005840; C:ribosome; 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; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 97 50S ribosomal protein L31. FT /FTId=PRO_0000173126. SQ SEQUENCE 97 AA; 10954 MW; C82719E15B6C9047 CRC64; MKKAIHFQSQ PVVFNCASCN SNFTIDSTAK QKDLAIDICG KCHPFYIGQL TKQTVHGRAE KLSQKFNAGK AFLENKTKKS NQAKVEKQTR HRSINEL // ID RL28_MYCGE Reviewed; 64 AA. AC P47665; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=50S ribosomal protein L28 {ECO:0000255|HAMAP-Rule:MF_00373}; GN Name=rpmB {ECO:0000255|HAMAP-Rule:MF_00373}; GN Synonyms=rpl28 {ECO:0000255|HAMAP-Rule:MF_00373}; GN OrderedLocusNames=MG426; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the ribosomal protein L28P family. CC {ECO:0000255|HAMAP-Rule:MF_00373}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC72447.1; -; Genomic_DNA. DR PIR; A64247; A64247. DR ProteinModelPortal; P47665; -. DR STRING; 243273.MgenG_010200000335; -. DR EnsemblBacteria; AAC72447; AAC72447; MG_426. DR KEGG; mge:MG_426; -. DR PATRIC; 20010438; VBIMycGen98045_0492. DR eggNOG; ENOG41084QT; Bacteria. DR eggNOG; COG0227; LUCA. DR KO; K02902; -. DR OMA; MGRCYIS; -. DR OrthoDB; EOG6W727M; -. DR BioCyc; MGEN243273:GH2R-480-MONOMER; -. DR Proteomes; UP000000807; 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_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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 64 50S ribosomal protein L28. FT /FTId=PRO_0000178504. SQ SEQUENCE 64 AA; 7486 MW; D4602C491A6D6FEA CRC64; MAKKDQLTLR GPLYGNNRSH SKTITRRKWN VNLQSCKIKD TNGKVTRILV STKTIRTLKK QNRF // ID RL5_MYCGE Reviewed; 180 AA. AC P47409; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333}; GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; GN Synonyms=rpl5 {ECO:0000255|HAMAP-Rule:MF_01333}; GN OrderedLocusNames=MG163; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71381.1; -; Genomic_DNA. DR PIR; A64218; A64218. DR RefSeq; WP_009885847.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47409; -. DR SMR; P47409; 1-179. DR STRING; 243273.MgenG_010200002204; -. DR EnsemblBacteria; AAC71381; AAC71381; MG_163. DR KEGG; mge:MG_163; -. DR PATRIC; 20009758; VBIMycGen98045_0185. DR eggNOG; ENOG4105CW6; Bacteria. DR eggNOG; COG0094; LUCA. DR KO; K02931; -. DR OMA; EQVMFHE; -. DR OrthoDB; EOG6M9F1R; -. DR BioCyc; MGEN243273:GH2R-172-MONOMER; -. DR Proteomes; UP000000807; 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:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. 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 1 180 50S ribosomal protein L5. FT /FTId=PRO_0000124949. SQ SEQUENCE 180 AA; 20450 MW; 068DAA2D579F69BB CRC64; MNNLEKTYKT ELVNQLQQQL GFSSIMQVPK LTKIVVNMGV GDAIRDNKFL ESALNELHLI TGQKPVATKA KNAISTYKLR AGQLIGCKVT LRNKKMWSFL EKLIYIALPR VRDFRGLSLR SFDGKGNYTI GIKEQIIFPE IVYDDIKRIR GFDITIVTST NKDSEALALL RALKMPFVKE // ID RL2_MYCGE Reviewed; 285 AA. AC P47400; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320}; GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; GN Synonyms=rpl2 {ECO:0000255|HAMAP-Rule:MF_01320}; GN OrderedLocusNames=MG154; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71372.1; -; Genomic_DNA. DR PIR; A64217; A64217. DR RefSeq; WP_009885838.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47400; -. DR SMR; P47400; 63-201. DR STRING; 243273.MgenG_010200002159; -. DR EnsemblBacteria; AAC71372; AAC71372; MG_154. DR KEGG; mge:MG_154; -. DR PATRIC; 20009740; VBIMycGen98045_0176. DR eggNOG; ENOG4105CFD; Bacteria. DR eggNOG; COG0090; LUCA. DR KO; K02886; -. DR OMA; HNRGVTM; -. DR OrthoDB; EOG6TR0J1; -. DR BioCyc; MGEN243273:GH2R-163-MONOMER; -. DR Proteomes; UP000000807; 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:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. 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 1 285 50S ribosomal protein L2. FT /FTId=PRO_0000129581. SQ SEQUENCE 285 AA; 31883 MW; 2B4F1275CD9E3907 CRC64; MAIKKIISRS NSGIHNATVI DFKKLLTNSK PEKSLLVTLK KHAGRNNQGK ITVRHHGGRH KRKYRLIDFK RYHYDNLKAT VKSIEYDPNR SCFISLLHYQ NGVKTYIISP DGIKVGDQVY SSDHAIDIKL GYCMPLAFIP EGTQVHNIEL NPKGGGKIAR SAGSYARILG QDETGKYIIL QLISGETRKF LKECRATVGV VSNLDHNLVV IGKAGRSRHK GIRPTVRGSA MNPNDHPHGG GEGRSPVGRD APRTPWGKRH MGVKTRNMKK HSTNLIIRNR KGEQY // ID RL34_MYCGE Reviewed; 48 AA. AC P47704; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=50S ribosomal protein L34; GN Name=rpmH; Synonyms=rpl34; OrderedLocusNames=MG466; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC72486.1; -; Genomic_DNA. DR PIR; E64251; E64251. DR RefSeq; WP_009885567.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47704; -. DR SMR; P47704; 1-48. DR STRING; 243273.MgenG_010200000085; -. DR EnsemblBacteria; AAC72486; AAC72486; MG_466. DR KEGG; mge:MG_466; -. DR PATRIC; 20010526; VBIMycGen98045_0536. DR eggNOG; ENOG4105VG0; Bacteria. DR eggNOG; COG0230; LUCA. DR KO; K02914; -. DR OrthoDB; EOG6DZF71; -. DR BioCyc; MGEN243273:GH2R-519-MONOMER; -. DR Proteomes; UP000000807; 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 48 50S ribosomal protein L34. FT /FTId=PRO_0000187414. SQ SEQUENCE 48 AA; 5707 MW; C91F03E39F447C0C CRC64; MKRTYQPSKL KRAKTHGFMA RMATAQGRKV LRQRRFKNRA QLTVSSER // ID RL7_MYCGE Reviewed; 122 AA. AC P36255; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 13-APR-2016, entry version 96. DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368}; GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; Synonyms=rpl7; GN OrderedLocusNames=MG362; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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. {ECO:0000255|HAMAP- CC Rule:MF_00368}. CC -!- SUBUNIT: Homodimer. Part of the ribosomal stalk of the 50S CC ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10 CC forms an elongated spine to which 2 to 4 L12 dimers bind in a CC sequential fashion. Binds GTP-bound translation factors. CC {ECO:0000255|HAMAP-Rule:MF_00368}. CC -!- SIMILARITY: Belongs to the ribosomal protein L7/L12P family. CC {ECO:0000255|HAMAP-Rule:MF_00368}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71588.1; -; Genomic_DNA. DR EMBL; U02206; AAD12497.1; -; Genomic_DNA. DR PIR; A64240; A64240. DR RefSeq; WP_009885819.1; NZ_AAGX01000006.1. DR ProteinModelPortal; P36255; -. DR STRING; 243273.MgenG_010200001963; -. DR EnsemblBacteria; AAC71588; AAC71588; MG_362. DR KEGG; mge:MG_362; -. DR PATRIC; 20010304; VBIMycGen98045_0426. DR eggNOG; ENOG41082SK; Bacteria. DR eggNOG; COG0222; LUCA. DR KO; K02935; -. DR OMA; CVVKQDI; -. DR OrthoDB; EOG6WMJ69; -. DR BioCyc; MGEN243273:GH2R-416-MONOMER; -. DR Proteomes; UP000000807; 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; 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 122 50S ribosomal protein L7/L12. FT /FTId=PRO_0000157552. SQ SEQUENCE 122 AA; 13060 MW; CFFB204E31F489F7 CRC64; MGKLDKKQLI ESLKEMTIVE IDEIIKAVEE AFGVTATPIV AAGAAGATQE AASEVSVKVT GYADNAKLAV LKLYREITGV GLMEAKTAVE KLPCVVKQDI KPEEAEELKK RFVEVGATVE VK // ID RL9_MYCGE Reviewed; 150 AA. AC P47339; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503}; GN Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; GN Synonyms=rpl9 {ECO:0000255|HAMAP-Rule:MF_00503}; GN OrderedLocusNames=MG093; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71311.1; -; Genomic_DNA. DR PIR; C64210; C64210. DR RefSeq; WP_009885649.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47339; -. DR STRING; 243273.MgenG_010200000690; -. DR EnsemblBacteria; AAC71311; AAC71311; MG_093. DR KEGG; mge:MG_093; -. DR PATRIC; 20009588; VBIMycGen98045_0103. DR eggNOG; ENOG41087V7; Bacteria. DR eggNOG; COG0359; LUCA. DR KO; K02939; -. DR OMA; HKLETHH; -. DR OrthoDB; EOG6D8BH0; -. DR BioCyc; MGEN243273:GH2R-96-MONOMER; -. DR Proteomes; UP000000807; 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; 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 1 150 50S ribosomal protein L9. FT /FTId=PRO_0000176651. SQ SEQUENCE 150 AA; 17380 MW; 50A19B6EAA48E8D6 CRC64; MKIILKQDVA KLGKRFDVVE VKDGFAIHFL FPKKLAAPLT KKAIANRDLF LKQQQEQYQK NRALAEKLKL VIEQTPLTFQ LKQHDGKPYG SIITKQIINL AKQQRLDLQR FMFKDNVRLQ FGEHKLILHL FEEITATLTV IVNPENGTTN // ID RL4_MYCGE Reviewed; 211 AA. AC P47398; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328}; GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; GN Synonyms=rpl4 {ECO:0000255|HAMAP-Rule:MF_01328}; GN OrderedLocusNames=MG152; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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. {ECO:0000255|HAMAP-Rule:MF_01328}. CC -!- FUNCTION: Forms part of the polypeptide exit tunnel. CC {ECO:0000255|HAMAP-Rule:MF_01328}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01328}. CC -!- SIMILARITY: Belongs to the ribosomal protein L4P family. CC {ECO:0000255|HAMAP-Rule:MF_01328}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71370.1; -; Genomic_DNA. DR PIR; H64216; H64216. DR RefSeq; WP_009885836.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47398; -. DR STRING; 243273.MgenG_010200002149; -. DR EnsemblBacteria; AAC71370; AAC71370; MG_152. DR KEGG; mge:MG_152; -. DR PATRIC; 20009736; VBIMycGen98045_0174. DR eggNOG; ENOG4106U5A; Bacteria. DR eggNOG; COG0088; LUCA. DR KO; K02926; -. DR OMA; HIIYLEI; -. DR OrthoDB; EOG6M0T9G; -. DR BioCyc; MGEN243273:GH2R-161-MONOMER; -. DR Proteomes; UP000000807; 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; 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; 1. DR Pfam; PF00573; Ribosomal_L4; 1. DR SUPFAM; SSF52166; SSF52166; 1. DR TIGRFAMs; TIGR03953; rplD_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 211 50S ribosomal protein L4. FT /FTId=PRO_0000129239. SQ SEQUENCE 211 AA; 23508 MW; 8791B46898954D23 CRC64; MAKLKVIQFD GSFKGEIQPA NHLLLKKAVI QPVFDAILLE QAACRQGTHS TLTKGEVSGG GKKPYKQKHT GKARQGSIRN PHYVGGGVVF GPKPNRNYKL KLNKKAYQLA LTSAFAQKLN NNQVIVAEAK LFEQTNAKTK KMLTFLKNAK LTEQKLLFVI DTISKPLLLS TNNLKQIVVK QFNKVSVRDL LLAKTIIIEK AAFTKLEERL K // ID RNM5_MYCGE Reviewed; 178 AA. AC P47303; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Ribonuclease M5; DE EC=3.1.26.8; DE AltName: Full=RNase M5; DE AltName: Full=Ribosomal RNA terminal maturase M5; GN Name=rnmV; OrderedLocusNames=MG057; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Required for correct processing of both the 5' and 3' CC ends of 5S rRNA precursor. Cleaves both sides of a double-stranded CC region yielding mature 5S rRNA in one step (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 21 CC and 42 nucleotides, respectively, from the 5'- and 3'-termini of a CC 5S-rRNA precursor. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00995}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribonuclease M5 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|PROSITE- CC ProRule:PRU00995}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71274.1; -; Genomic_DNA. DR PIR; C64206; C64206. DR RefSeq; WP_009885722.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47303; -. DR STRING; 243273.MgenG_010200001175; -. DR EnsemblBacteria; AAC71274; AAC71274; MG_057. DR KEGG; mge:MG_057; -. DR PATRIC; 20009496; VBIMycGen98045_0058. DR eggNOG; ENOG4105HVR; Bacteria. DR eggNOG; COG1658; LUCA. DR KO; K05985; -. DR OMA; ITKNANQ; -. DR OrthoDB; EOG6XQ3R3; -. DR BioCyc; MGEN243273:GH2R-59-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043822; F:ribonuclease M5 activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01469; RNase_M5; 1. DR InterPro; IPR004466; RNase_M5. DR InterPro; IPR025156; RNase_M5_C. DR InterPro; IPR006171; Toprim_domain. DR Pfam; PF13331; DUF4093; 1. DR Pfam; PF01751; Toprim; 1. DR SMART; SM00493; TOPRIM; 1. DR TIGRFAMs; TIGR00334; 5S_RNA_mat_M5; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Magnesium; KW Metal-binding; Nuclease; Reference proteome; Ribosome biogenesis; KW RNA-binding; rRNA processing; rRNA-binding. FT CHAIN 1 178 Ribonuclease M5. FT /FTId=PRO_0000210401. FT DOMAIN 10 94 Toprim. {ECO:0000255|PROSITE- FT ProRule:PRU00995}. FT METAL 16 16 Magnesium 1; catalytic. FT {ECO:0000255|PROSITE-ProRule:PRU00995}. FT METAL 62 62 Magnesium 1; catalytic. FT {ECO:0000255|PROSITE-ProRule:PRU00995}. FT METAL 62 62 Magnesium 2. {ECO:0000255|PROSITE- FT ProRule:PRU00995}. FT METAL 64 64 Magnesium 2. {ECO:0000255|PROSITE- FT ProRule:PRU00995}. SQ SEQUENCE 178 AA; 20497 MW; 49C5D330D420E64A CRC64; MDQKARIKID GVIVCEGKTD QAKLQQIFDV DVITTNGSAL KKETINLIKK ISEKQTVILL LDPDQQGKKI RSKLEQHLTN YYNCYVDMNA RLKNAKKAGI AEMETSALIA ALNNRVAITK NANQSILWDQ YLSLKLNDKK KRLLLCNNLN LPYFNHKQLF KKLNLLNLTF QDVWKHLK // ID RL6_MYCGE Reviewed; 184 AA. AC P47412; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365}; GN Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; GN Synonyms=rpl6 {ECO:0000255|HAMAP-Rule:MF_01365}; GN OrderedLocusNames=MG166; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71384.1; -; Genomic_DNA. DR PIR; D64218; D64218. DR RefSeq; WP_010869360.1; NC_000908.2. DR ProteinModelPortal; P47412; -. DR STRING; 243273.MgenG_010200002229; -. DR EnsemblBacteria; AAC71384; AAC71384; MG_166. DR KEGG; mge:MG_166; -. DR PATRIC; 20009764; VBIMycGen98045_0188. DR eggNOG; ENOG4108R5J; Bacteria. DR eggNOG; COG0097; LUCA. DR KO; K02933; -. DR OMA; LIANMVE; -. DR OrthoDB; EOG67DPRD; -. DR BioCyc; MGEN243273:GH2R-175-MONOMER; -. DR Proteomes; UP000000807; 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; 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 InterPro; IPR002358; Ribosomal_L6_CS. 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. DR PROSITE; PS00525; RIBOSOMAL_L6_1; 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_0000131059. SQ SEQUENCE 184 AA; 20523 MW; 5460B09C1E4D14A1 CRC64; MSKIGNRSIK IDPSKVSLMQ TTTLLTIKGP LGENTIKLPK NLPLKFVVEN DTIKVTNNNN LKQTKILHGT FNALVNNAVI GVTKGFEKKL ILVGVGYRAN VEGQFLNLQL GYSHPIKELI PNQLTVKVEK NTEITISGIK KELVGQFATE IRKWRKPEPY KGKGVLYFNE VIVRKQGKTA EGKK // ID RNPA_MYCGE Reviewed; 128 AA. AC P47703; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 93. 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}; OrderedLocusNames=MG465; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC72485.1; -; Genomic_DNA. DR PIR; D64251; D64251. DR ProteinModelPortal; P47703; -. DR STRING; 243273.MgenG_010200000090; -. DR EnsemblBacteria; AAC72485; AAC72485; MG_465. DR KEGG; mge:MG_465; -. DR PATRIC; 20010524; VBIMycGen98045_0535. DR eggNOG; COG0594; LUCA. DR KO; K03536; -. DR OMA; TFINAYF; -. DR OrthoDB; EOG654P5P; -. DR BioCyc; MGEN243273:GH2R-518-MONOMER; -. DR BRENDA; 3.1.26.5; 3528. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; RNA-binding; tRNA processing. FT CHAIN 1 128 Ribonuclease P protein component. FT /FTId=PRO_0000198486. SQ SEQUENCE 128 AA; 15178 MW; A8CA9F8C8E676A16 CRC64; MLNSRFPVSV KKSHSLRERK VFTTILQSKT RFFGTFINAY FIKNNHSTWR VAISIAKTKY KLAVQRNLIK RQIRSIFQQI SNNLEPWDIL VIVNKGFIEL TFKEKQKLFL QLLKRIKEVD AYQTSANK // ID RNR_MYCGE Reviewed; 725 AA. AC P47350; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 98. 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=MG104; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-163. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71322.1; -; Genomic_DNA. DR EMBL; U01795; AAD12320.1; -; Genomic_DNA. DR PIR; E64211; E64211. DR RefSeq; WP_009885662.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47350; -. DR STRING; 243273.MgenG_010200000765; -. DR EnsemblBacteria; AAC71322; AAC71322; MG_104. DR KEGG; mge:MG_104; -. DR PATRIC; 20009612; VBIMycGen98045_0115. DR eggNOG; ENOG4105C40; Bacteria. DR eggNOG; COG0557; LUCA. DR KO; K12573; -. DR OMA; IENFVVF; -. DR OrthoDB; EOG6Q5NRD; -. DR BioCyc; MGEN243273:GH2R-108-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. 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; 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; PF00575; S1; 1. DR SMART; SM00357; CSP; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 3. 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 1 725 Ribonuclease R. FT /FTId=PRO_0000166408. FT DOMAIN 644 725 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_01895}. SQ SEQUENCE 725 AA; 82899 MW; CC145605C4ADCCBB CRC64; MKVLTELQKQ IFTIVKKENG KPIPPGIVVR MMENSPNFPG KHLIYRAIDD LLDWAILRKA GGVTNQLLVN YEPAEPLLDK KLQGILTLGN KNSGFIRSLD DDKTVYYVHY SNLTGALDGD LVEFCKLDKP QFGDKFDAAV ITILKRARIL YAGNFLVDQN EFALEYKIVA DNPRFYLTMI VNPDSIPNNL ASNTKIAFQI DEYDPDNNLC KVSVQQVLGN NDDPLINIKA IMLDNSIVFE TNDVVEQHAN KLSFDTEEQH KAYRQDLTDL AFVTVDPTTS KDLDDAIYVK TIPTGFVLYV AIADVAHYVN RNSEIDIEAK HKTSSIYLPG HYVVPMLPEQ LSNQLCSLNP AQKRYVVVCE ISFDNQGRIK TNKLYPATII SKNRFSYDQV NKWLNNKSEL NCDETVINSL KAAFTLSDLI QAQRQKRGTI DLSHKETEIV VDEHYFPIKI NFLVHDKAET MIENLMVVAN ETVAWVLTNN KIALPYRVHP RPSKKKLQSL IETVGELNIT KPQFNLDTVT SSQIASWLNE NKDNPSYEIF VILLLRTLGK AFYSVNPLMH FSIGSNHYTH FTSPIRRYID LTIHRLLWMH LFTPDQFTDN ERDQLKQELE KIADTVNDTE IKIINCERNA NDYLTTLLLS KQIGKTFSGF ISAITSFGIF MRMDENNFDG LIKITTIPDD FFIFEKEKMV LKGRKTNKVY KIGDRLEAKL SEIDFIQKRA ILTLI // ID RNY_MYCGE Reviewed; 484 AA. AC P47376; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 94. 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=MG130; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71348.1; -; Genomic_DNA. DR PIR; D64214; D64214. DR RefSeq; WP_010869346.1; NC_000908.2. DR ProteinModelPortal; P47376; -. DR STRING; 243273.MgenG_010200000920; -. DR EnsemblBacteria; AAC71348; AAC71348; MG_130. DR KEGG; mge:MG_130; -. DR PATRIC; 20009664; VBIMycGen98045_0141. DR eggNOG; ENOG4105E4Y; Bacteria. DR eggNOG; COG1418; LUCA. DR KO; K18682; -. DR OMA; KYTIANH; -. DR OrthoDB; EOG6QCD98; -. DR BioCyc; MGEN243273:GH2R-134-MONOMER; -. DR Proteomes; UP000000807; 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 HAMAP; MF_00335; RNase_Y; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR006675; HDIG_dom. DR InterPro; IPR017705; Ribonuclease_Y. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00277; HDIG; 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 1 484 Ribonuclease Y. FT /FTId=PRO_0000163782. FT TRANSMEM 18 38 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00335}. FT DOMAIN 166 234 KH. {ECO:0000255|HAMAP-Rule:MF_00335}. FT DOMAIN 293 384 HD. {ECO:0000255|HAMAP-Rule:MF_00335}. SQ SEQUENCE 484 AA; 56033 MW; 82A95B1EDF6C481C CRC64; MNNNITNSIA QLFFNTSFFA FLFLIIIAFN LCLFAYLYFQ YRIYKKNPKK ANNFKANEYE KIKLLKNQNF TESNKLIATT NELNELTSQL DNILVRIINK PLAKLVNDFL DEQIKQIVKL DKNSSDFHSE SDNLPFYTKL FNDFHFGVDK LININIKNPL YNWVYSPSFL ISESDFRKLN GISGINKKLL VEKLRIEDIV FTDLNKKYEV NVLTESPIKA QKTVLTVRNI LMNDYVDNER IESYVQQANF FFTEHCKKIG KEILESLNIF ISSSSLHRHF GFLAFRYSFG QNVLSHSLET AFLTAHLAAL IELDSELSLK CGLLHDIGKS NDDNGKESHT ITGAKLAEQF QLPDDIKYTI ANHHNKHIDN TYCRLTQIAD KLSAARIGAR SDSSLLFKQL KDELKKIVDK TINNFHTTIL LGQSGRRLMI WLETKNQNQL LSNEQIIEMV EKIKAEIAKN PITNHFPIKV VIRYNFEHSF NTKS // ID RNJ_MYCGE Reviewed; 569 AA. AC P47385; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=Ribonuclease J {ECO:0000255|HAMAP-Rule:MF_01491}; DE Short=RNase J {ECO:0000255|HAMAP-Rule:MF_01491}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01491}; GN Name=rnj {ECO:0000255|HAMAP-Rule:MF_01491}; OrderedLocusNames=MG139; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly CC endoonuclease activity. Involved in maturation of rRNA and in some CC organisms also mRNA maturation and/or decay (By similarity). CC {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01491}; CC Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if CC Zn(2+) or Mg(2+) is physiologically important. {ECO:0000255|HAMAP- CC Rule:MF_01491}; CC -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome. CC {ECO:0000255|HAMAP-Rule:MF_01491}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}. CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC RNA-metabolizing metallo-beta-lactamase-like family. Bacterial CC RNase J subfamily. {ECO:0000255|HAMAP-Rule:MF_01491}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71357.1; -; Genomic_DNA. DR PIR; D64215; D64215. DR RefSeq; WP_009885694.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47385; -. DR STRING; 243273.MgenG_010200000975; -. DR PRIDE; P47385; -. DR EnsemblBacteria; AAC71357; AAC71357; MG_139. DR KEGG; mge:MG_139; -. DR PATRIC; 20009684; VBIMycGen98045_0151. DR eggNOG; ENOG4105CN5; Bacteria. DR eggNOG; COG0595; LUCA. DR KO; K12574; -. DR OMA; GEFRMQR; -. DR OrthoDB; EOG6P5ZDC; -. DR BioCyc; MGEN243273:GH2R-143-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:InterPro. DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.60.15.10; -; 1. DR HAMAP; MF_01491; RNase_J_bact; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR011108; RMMBL. DR InterPro; IPR004613; RNase_J. DR InterPro; IPR030854; RNase_J_bac. DR InterPro; IPR001587; RNase_J_CS. DR PANTHER; PTHR11203:SF22; PTHR11203:SF22; 1. DR Pfam; PF00753; Lactamase_B; 1. DR Pfam; PF07521; RMMBL; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR00649; MG423; 1. DR PROSITE; PS01292; UPF0036; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Exonuclease; Hydrolase; KW Metal-binding; Nuclease; Reference proteome; RNA-binding; KW rRNA processing; Zinc. FT CHAIN 1 569 Ribonuclease J. FT /FTId=PRO_0000215271. FT REGION 373 377 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 81 81 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 83 83 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 85 85 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 86 86 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 150 150 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 172 172 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 172 172 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. FT METAL 399 399 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01491}. SQ SEQUENCE 569 AA; 64201 MW; D3C9EB4643F0E59B CRC64; MIKDFNPGDF IGKKPTKIYA FGGIQEVGKN MYGIEYDDEI IIIDCGIKFA SDDLLGINGI IPSFEHLIEN QSKVKALFIT HGHEDHIGGV PYLLKQVDIP VIYAPRIAAS LILKKVNEHK DAKLNKIVTF DDFSEFQTKH FKIDFYRVNH SIPDAFGICV QTPNGNIVQS GDYRFDFAAG SEMLDVHKVV KIAERNVHVF MSESTNAEVP GFSQSEKLIY RNIQKILKEA RGRVILTTFA SNITRINEII EIALNNKRKI CLLGKSMDVN VNISRKIGLM AIDSNDIVEV RDIKNYPDRN ILILCTGSQG EEAAALNTMA RGKHNWVSLK STDTIIMSSN PIPGNYAAVE NLLNELSKFG VAIYENSSQL KLHASGHATQ QELQLMLNLM FPKYLIPIHG EFKMMRTIKN IANECGIKSE DVALLSNGQV MYLIDEELYY SNEIINADPI YIESHNSSPD LARIIKQRQI LSRDGMFAVI VVFDKNNNII GIPTLITRGC FFALDSNPLM TKIAHSVKRT LESVIQSKKF NSHEQLTKEL KRVCKETVSY FIWKNKNRNP LISTVLSWI // ID RPOB_MYCGE Reviewed; 1390 AA. AC P47583; Q49439; Q49441; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 104. 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}; OrderedLocusNames=MG341; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 533-644 AND 945-1067. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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_01321}. 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; L43967; AAC71566.1; -; Genomic_DNA. DR EMBL; U01737; AAD10547.1; -; Genomic_DNA. DR EMBL; U01735; AAD10545.1; -; Genomic_DNA. DR PIR; G64237; G64237. DR RefSeq; WP_009885798.1; NZ_AAGX01000006.1. DR ProteinModelPortal; P47583; -. DR STRING; 243273.MgenG_010200001808; -. DR EnsemblBacteria; AAC71566; AAC71566; MG_341. DR KEGG; mge:MG_341; -. DR PATRIC; 20010248; VBIMycGen98045_0401. DR eggNOG; ENOG4108IIJ; Bacteria. DR eggNOG; COG0085; LUCA. DR KO; K03043; -. DR OMA; DIRDVHY; -. DR OrthoDB; EOG6M9DS6; -. DR BioCyc; MGEN243273:GH2R-391-MONOMER; -. DR Proteomes; UP000000807; 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: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; -; 3. 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; 4. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 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 1390 DNA-directed RNA polymerase subunit beta. FT /FTId=PRO_0000047919. FT CONFLICT 1062 1062 H -> L (in Ref. 2; AAD10545). FT {ECO:0000305}. SQ SEQUENCE 1390 AA; 156331 MW; 4D1888A07680912C CRC64; MSQKSNFFQK RYSPTATRRY YGKIETNFIQ PNLADIQIKS YQKFLDHDLE KLIASYFPIK SPNDRYTINF RGLHRTEPER DEAQSRAQSK TYEVGIYADL ELVDNDKGTV KKARKSKKNI ASNTNGVFLA SMPLITHDGV FIINGIEKFV ISQITRSPGI YMLTKSQLKL SNSRKRVQEG YVCEVLPANG SVMLIYISNK KKIEDAFVQI LLRDAVREGA KIFPITTLLK AFGLNNREIL KIFKNNEFIK RSLEAEIYNA KDFLSNVDPE IKNLLKEFRD GKTDLRRKGI ASDQKLRSLV NEYVTLEKQY NALKQTSPND SSLTALELEM ENKMDSVITE RAAKHIVNEL SISLRDIENT EECHEVSFHA LLCARFFRNK RYNLSNAGRY KVSRKLRLTE RIYQKTLACD LFLKDGKLLL KKGTLLLKEE IDKIKQAAKN NEISFVNKMQ LTTDGKAVDL AKESLFYETI DVYITNDNLS VSVPVIGIHN ENDLNKAMTL SDFIASISYV INLPYGIGKY DDIDHLGNKR VKLINELITA KLESGFTRME RFLKEKLTIA DGVNRGQQIN EEGQVIEQGE KKELTIKSLI NSKPIQIVIK DFFNTHQLTQ FLDHQNPLSE LSNKRRISAM GPGGISREDP NLDIRDVHYS QYGRICPIET PEGMNIGLIM SLASFAKIDE NGFLMAPYRK IKAGVITDEV EYLTALREDE HIIAEISSLV NISNDNKILD KEIIGRYRSM QGLYDPLKID YIDVAPHQVV SIGSSLIPFL ENDDSARALM GTNMQRQAYP LIKPYAPAVG TGQEHKIASD SGLTMSSPCS GVVSYVDNSK IIITSDSSKK ETVNLVKFER SNQNTCYNHK PIVEIGQRVN KDEIIVDGPA VNKSELALGQ NVLVAFTTWN GYNYEDAIVI SERLVKEDIL TSLTINEYVA QCLSTKNGDE QITRDIPNVS DANKRYLDEN GIIMVGAEVK EGDVLVGKVS PKGQVEVSPE EKLFKAIFPE SVQNVRDSSL KVSHGGDGIV SAVKRFSIAN GDELNDGVIE MIKVYVVQKR KIQIGDKLAG RHGNKGVISK VVPIEDMPHL EDGTPVDILL NPLGVPSRMN IGQIFETHLG YAAHKLAVRS LISSCFDQNK AKEFAIEINQ PQARVERLIK GLKNQINDRN IKSEKEALEK LDNSDISLVL KEIGMSFDDL IYKIATPIFQ GVNFLDLQDV MQEAGLDPQK NQGKFKLIDG RSGMPFERPI SLGIMYMMKL NHMVDDKIHA RAVGPYSKIT QQPLGGKSQN GGQRFGEMEV WALEAYGAAY NLQELLTIKS DDVQGRNRAY AAIVKGAAFP EPGIPESFKL LTKELQGLAL SVSFIYDDNT QQDSNNVSIL QSDGEQDEFF NDFEFDTEGY // ID RPOE_MYCGE Reviewed; 145 AA. AC P47268; Q49195; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Probable DNA-directed RNA polymerase subunit delta; DE AltName: Full=RNAP delta factor; GN Name=rpoE; OrderedLocusNames=MG022; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Participates in both the initiation and recycling phases CC of transcription. In the presence of the delta subunit, RNAP CC displays an increased specificity of transcription, a decreased CC affinity for nucleic acids, and an increased efficiency of RNA CC synthesis because of enhanced recycling (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: RNAP is composed of a core of 2 alpha, a beta and a beta' CC subunits. The core is associated with a delta subunit and one of CC several sigma factors (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RpoE family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC43196.1; 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; L43967; AAC71238.1; -; Genomic_DNA. DR EMBL; U01721; AAC43196.1; ALT_INIT; Unassigned_DNA. DR PIR; D64202; D64202. DR RefSeq; WP_009885918.1; NZ_AAGX01000010.1. DR STRING; 243273.MgenG_010200002771; -. DR EnsemblBacteria; AAC71238; AAC71238; MG_022. DR KEGG; mge:MG_022; -. DR PATRIC; 20009420; VBIMycGen98045_0020. DR eggNOG; COG3343; LUCA. DR KO; K03048; -. DR OrthoDB; EOG6S26DH; -. DR BioCyc; MGEN243273:GH2R-22-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; 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:InterPro. DR HAMAP; MF_00357; RNApol_bact_RpoE; 1. DR InterPro; IPR007759; HB1/Asxl_HTH. DR InterPro; IPR029757; RpoE. DR Pfam; PF05066; HARE-HTH; 1. DR TIGRFAMs; TIGR04567; RNAP_delt_lowGC; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 145 Probable DNA-directed RNA polymerase FT subunit delta. FT /FTId=PRO_0000204318. FT COMPBIAS 93 145 Asp/Glu-rich (acidic). SQ SEQUENCE 145 AA; 17057 MW; C7A1901C94E2A41F CRC64; MQLEYLNLIS QAKVIAEKQF KANPFSFETI WKEVVKHFKI SKQDEPSLIG RFYQDFLEDP NFVYLGDRKW KLRDFMKFDE WNKISQSMFV TKEIFEEGYE DLSNKKVEPE EGVGDFIMGN DGDDNETGSE IVQGLINDSF SEENQ // ID RNC_MYCGE Reviewed; 262 AA. AC P47607; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Ribonuclease 3 {ECO:0000255|HAMAP-Rule:MF_00104}; DE EC=3.1.26.3 {ECO:0000255|HAMAP-Rule:MF_00104}; DE AltName: Full=Ribonuclease III {ECO:0000255|HAMAP-Rule:MF_00104}; DE Short=RNase III {ECO:0000255|HAMAP-Rule:MF_00104}; GN Name=rnc {ECO:0000255|HAMAP-Rule:MF_00104}; OrderedLocusNames=MG367; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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). Processes some mRNAs, and CC tRNAs when they are encoded in the rRNA operon. Processes pre- CC crRNA and tracrRNA of type II CRISPR loci if present in the CC organism. {ECO:0000255|HAMAP-Rule:MF_00104}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_00104}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00104}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00104}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00104}. CC -!- SIMILARITY: Contains 1 RNase III domain. {ECO:0000255|HAMAP- CC Rule:MF_00104}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71594.1; -; Genomic_DNA. DR PIR; F64240; F64240. DR ProteinModelPortal; P47607; -. DR STRING; 243273.MgenG_010200002008; -. DR EnsemblBacteria; AAC71594; AAC71594; MG_367. DR KEGG; mge:MG_367; -. DR PATRIC; 20010316; VBIMycGen98045_0432. DR eggNOG; ENOG4107SU0; Bacteria. DR eggNOG; COG0571; LUCA. DR KO; K03685; -. DR OMA; HEDVSES; -. DR OrthoDB; EOG6T1WVS; -. DR BioCyc; MGEN243273:GH2R-422-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-HAMAP. 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 HAMAP; MF_00104; RNase_III; 1. DR InterPro; IPR011907; RNase_III. DR InterPro; IPR000999; RNase_III_dom. DR Pfam; PF14622; Ribonucleas_3_3; 1. DR SMART; SM00535; RIBOc; 1. DR SUPFAM; SSF69065; SSF69065; 1. DR TIGRFAMs; TIGR02191; RNaseIII; 1. DR PROSITE; PS00517; RNASE_3_1; 1. DR PROSITE; PS50142; RNASE_3_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Magnesium; KW Metal-binding; mRNA processing; Nuclease; Reference proteome; KW rRNA processing; tRNA processing. FT CHAIN 1 262 Ribonuclease 3. FT /FTId=PRO_0000180410. FT DOMAIN 18 141 RNase III. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT ACT_SITE 63 63 {ECO:0000255|HAMAP-Rule:MF_00104}. FT ACT_SITE 130 130 {ECO:0000255|HAMAP-Rule:MF_00104}. FT METAL 59 59 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT METAL 127 127 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT METAL 130 130 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. SQ SEQUENCE 262 AA; 30338 MW; B54D2A893EA01CBE CRC64; MKNKVLKLKN NKIFDKKLAT FLKNLDIFPN NWEFFEKAFI HASYINEHED VSESYDRLEF LGDALIDFVV AKKLFELYPK YNEGLLTRTK IEIVKGENLN RIGMELKLGD FVKLSNGAEL TENTVGDVLE ALVGAIYEDM GMKKATEFVE KYIFERTFSE ILKYDFFSLF QEQKLPEPRV RVSLTSNNLV LSIIELDGDI IWSQAIPNNK NYDDKSVLEH NAMASFTSFL KSSKGSHFFS DLKEKIENQK MCKKLAIKPK KN // ID RPOC_MYCGE Reviewed; 1292 AA. AC P47582; Q49292; Q49454; Q49483; Q49486; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 102. 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}; OrderedLocusNames=MG340; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-142 AND 1029-1148. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-506. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). 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_01322}. 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; L43967; AAC71565.1; -; Genomic_DNA. DR EMBL; U01797; AAD12323.1; -; Genomic_DNA. DR EMBL; U02169; AAD12451.1; -; Genomic_DNA. DR EMBL; X61528; CAB98132.1; -; Genomic_DNA. DR EMBL; X61534; CAA43746.1; ALT_SEQ; Genomic_DNA. DR PIR; F64237; F64237. DR ProteinModelPortal; P47582; -. DR STRING; 243273.MgenG_010200001803; -. DR EnsemblBacteria; AAC71565; AAC71565; MG_340. DR KEGG; mge:MG_340; -. DR PATRIC; 20010246; VBIMycGen98045_0400. DR eggNOG; ENOG4105D27; Bacteria. DR eggNOG; COG0086; LUCA. DR KO; K03046; -. DR OrthoDB; EOG6M9DS6; -. DR BioCyc; MGEN243273:GH2R-390-MONOMER; -. DR Proteomes; UP000000807; 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; 1. DR Pfam; PF00623; RNA_pol_Rpb1_2; 1. 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. DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 1292 DNA-directed RNA polymerase subunit FT beta'. FT /FTId=PRO_0000067759. FT CONFLICT 33 36 WSEG -> LIWR (in Ref. 2; AAD12323). FT {ECO:0000305}. FT CONFLICT 338 344 NDRLRRI -> KWPIKKD (in Ref. 3). FT {ECO:0000305}. FT CONFLICT 1029 1037 LTMRTFHTG -> MDNAYFPYW (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 1292 AA; 145659 MW; 15003759D34D17A5 CRC64; MTTTRRNKRN NKLYKNIKAI KLSIASNDTI LNWSEGEVTK AETINYKSLK PEPGGLFDEA IFGPVKDYEC ACGKFKKIKY RGVRCDRCGV WVTESIVRRE RMGHIALVSP VAHIWMSKEL PSPSKISLVL NISYKEVEQV LYFVNYIVLD TGKIKDDKIM PFKFKEVLDL TGKGSLSTRQ KMRRVIGYIF RNLIKSKSSE DYRKGKIFYE SLKNSSLPFS LNDAFNYIKK YTGFRVGIGA EAILELLNKI DLNLEFSRLN DALRKAKKDS VEDAKVKKIL RQLETISWFR NSKLHPKNMI LHTVPVIPPD IRPIIQLDGA KFTTSDINNF YRRVIIRNDR LRRILEDGTV PSIVVNNEKR LLQESVDALF DNSSRHKPSL SKDKRSLKSL TDRLKGKQGL FRHNLLGKRV DYSGRSVIVV GPELKMYEVG IPALMILKLF KPFIIHGLIN KFDENGNEIR PIAASIRQAE DMIKNQDDLI WGIVYDVIKD RPVLLNRAPT LHRLGIQAFE PRIVDGKAIR LHPLVTTAFN ADFDGDQMAV HVPLSENAVN EARAVLLASK HILGLKDGRP IVTPTQDMVL GNYYLTTERK GQLGEGIIFS TVYEARAAYE SQKVHLHAIV GISTKAFPNK KFACQGTLIT TVGKIIFNDV LGNNVPYIND GEFDENACPE KFIVKQGEDV RQSILKHQII PAFSKKVISK LIDLLYLLLE FKDLPKTLDN IKALGFKYST FSSTTVSVFD IPKYTNKQNY FDSADQQVLK YKQFYNKGLL TDDERYKRVV KLWNNVKEKV SDEIQNLIKQ EQYRDNSIVV MADSGARGNI SNFTQLFGMR GLMSKSFNYE RNNQSKIIKD TIEVPIKHSF FEGLTINEYF NSSYGARKGM TDTAMKTAKS GYMTRKLVDA THELIINHDD CGTRKGIVVE AIVETKTKSL IESLFDRIVN RYSITPIVDP ETQKTIVEAN SLITTQLAKQ ICATSIKEVL VRSVIYCERE NGICQYCFGI DLSTGKLVEL GTAVGVIAAQ SIGEPGTQLT MRTFHTGGVS TENNLAQGFE RLKQIFEVVT PKDFEKAVIS EVKGTVKSIT TVQNAQEVVI KSNVDERIYT IPFSAQIRVH VGDQVSPGSK ITEGSVDIKQ LLRIAGIQRV RQYMIVEIQK VYRIQGIDIA DKYVEIIIRQ LTNLLQVTDA GNSNLFVGQL VHSHYLNELN KSLLLAGKMP VIAINQVFGI DEAASKSNSF LSAASFQDTK KILTDAAVKN QVDYLLGLKE NVIIGGKIPA GTGFLTDEEL TFLGSKTVAE EY // ID RPOA_MYCGE Reviewed; 328 AA. AC P47423; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 106. 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}; OrderedLocusNames=MG177; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71396.1; -; Genomic_DNA. DR PIR; F64219; F64219. DR RefSeq; WP_009885862.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47423; -. DR STRING; 243273.MgenG_010200002289; -. DR EnsemblBacteria; AAC71396; AAC71396; MG_177. DR KEGG; mge:MG_177; -. DR PATRIC; 20009786; VBIMycGen98045_0199. DR eggNOG; ENOG4105CTF; Bacteria. DR eggNOG; COG0202; LUCA. DR KO; K03040; -. DR OMA; LMKFRNF; -. DR OrthoDB; EOG68WR84; -. DR BioCyc; MGEN243273:GH2R-186-MONOMER; -. DR Proteomes; UP000000807; 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 1 328 DNA-directed RNA polymerase subunit FT alpha. FT /FTId=PRO_0000175336. FT REGION 1 244 Alpha N-terminal domain (alpha-NTD). FT {ECO:0000255|HAMAP-Rule:MF_00059}. FT REGION 261 328 Alpha C-terminal domain (alpha-CTD). FT {ECO:0000255|HAMAP-Rule:MF_00059}. SQ SEQUENCE 328 AA; 36890 MW; 78371426889525A1 CRC64; MEKFLKYEIK VNNNQPTNTN PNYGIFEVAP LESGFGITIG NAMRRVLLSC IPGASVFAIA ISGVKQEFSN VEGVLEDVTE MVLNFKQLVV RISDLLFEDG EMIEPPLERW PVLKVTAEKK GAVYAKDLEC PAGFEVINKD LYLFSLQKDM KLTVSVYVKQ GRGFTSFLEN RELINSLGII ATDANFSPVL HCGYEVQEVK TSKQKLTDHL TFKIATNGAI KAVDAFAMAA KILIEHLNPI VSVNESIKNL TIIQEKAEER KVKSFAKQIE ELDFTVRTFN CLKRSGIHTL QELLSKSLTD IREIRNLGKK SEREIIKKVQ ELGLKFRS // ID RPE_MYCGE Reviewed; 209 AA. AC P47358; Q49304; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=Probable ribulose-phosphate 3-epimerase; DE EC=5.1.3.1; DE AltName: Full=Pentose-5-phosphate 3-epimerase; DE Short=PPE; DE AltName: Full=R5P3E; GN Name=rpe; OrderedLocusNames=MG112; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-157. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5- CC phosphate to D-xylulose 5-phosphate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = D-xylulose 5- CC phosphate. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 divalent metal cation per subunit. Active with CC Co(2+), Fe(2+), Mn(2+) and Zn(2+). {ECO:0000250}; CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase 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; L43967; AAC71330.1; -; Genomic_DNA. DR EMBL; U02181; AAD12467.1; -; Genomic_DNA. DR PIR; D64212; D64212. DR RefSeq; WP_009885669.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47358; -. DR STRING; 243273.MgenG_010200000810; -. DR EnsemblBacteria; AAC71330; AAC71330; MG_112. DR KEGG; mge:MG_112; -. DR PATRIC; 20009628; VBIMycGen98045_0123. DR eggNOG; ENOG4105DJV; Bacteria. DR eggNOG; COG0036; LUCA. DR KO; K01783; -. DR OMA; RISFHVE; -. DR OrthoDB; EOG67HK17; -. DR BioCyc; MGEN243273:GH2R-116-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. 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 SUPFAM; SSF51366; SSF51366; 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; Cobalt; Complete proteome; Iron; Isomerase; KW Manganese; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 209 Probable ribulose-phosphate 3-epimerase. FT /FTId=PRO_0000171575. FT REGION 143 146 Substrate binding. {ECO:0000250}. FT REGION 191 192 Substrate binding. {ECO:0000250}. FT ACT_SITE 35 35 Proton acceptor. {ECO:0000250}. FT ACT_SITE 170 170 Proton donor. {ECO:0000250}. FT METAL 33 33 Divalent metal cation. {ECO:0000250}. FT METAL 35 35 Divalent metal cation. {ECO:0000250}. FT METAL 64 64 Divalent metal cation. {ECO:0000250}. FT METAL 170 170 Divalent metal cation. {ECO:0000250}. FT BINDING 8 8 Substrate. {ECO:0000250}. FT BINDING 64 64 Substrate. {ECO:0000250}. FT BINDING 172 172 Substrate; via amide nitrogen. FT {ECO:0000250}. SQ SEQUENCE 209 AA; 24100 MW; 2A93610D3E1E4AB7 CRC64; MATKVVFSLL PLLNRFDKSL LESYFQDGLR LIHYDVMDQF VHNTAFKGEY LDELKTIGFD VNVHLMVEQI IPQINFYLSQ PNVKRISFHV EPFSFAKIKE LIQLVKENGK EVGLAFKFTT NLQLYQPFFT TIDFITLMSV PPGKGGQAFN EAVFTNLKIA NHYNLKIEID GGIKVNNIDQ IKAFVDFIVM GSGFIKLEQW QRQKLLQTI // ID RPIB_MYCGE Reviewed; 152 AA. AC P47636; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Probable ribose-5-phosphate isomerase B; DE EC=5.3.1.6; DE AltName: Full=Phosphoriboisomerase B; GN Name=rpiB; OrderedLocusNames=MG396; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate = D-ribulose 5-phosphate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative CC stage): step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LacAB/RpiB 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; L43967; AAC71624.1; -; Genomic_DNA. DR PIR; H64243; H64243. DR RefSeq; WP_009885626.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47636; -. DR STRING; 243273.MgenG_010200000525; -. DR EnsemblBacteria; AAC71624; AAC71624; MG_396. DR KEGG; mge:MG_396; -. DR PATRIC; 20010380; VBIMycGen98045_0463. DR eggNOG; ENOG4108YZG; Bacteria. DR eggNOG; COG0698; LUCA. DR KO; K01808; -. DR OMA; DYPDFVH; -. DR OrthoDB; EOG679TJ4; -. DR BioCyc; MGEN243273:GH2R-453-MONOMER; -. DR UniPathway; UPA00115; UER00412. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. 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 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Isomerase; KW Reference proteome. FT CHAIN 1 152 Probable ribose-5-phosphate isomerase B. FT /FTId=PRO_0000208165. FT REGION 70 75 Substrate binding. {ECO:0000250}. FT ACT_SITE 69 69 Proton acceptor. {ECO:0000255}. FT ACT_SITE 102 102 Proton donor. {ECO:0000250}. FT BINDING 11 11 Substrate. {ECO:0000250}. FT BINDING 113 113 Substrate. {ECO:0000250}. FT BINDING 136 136 Substrate. {ECO:0000250}. FT BINDING 140 140 Substrate. {ECO:0000250}. SQ SEQUENCE 152 AA; 16893 MW; 1D5A15E5C14F74DB CRC64; MSFNIFIASD HTGLTLKKII SEHLKTKQFN VVDLGPNYFD ANDDYPDFAF LVADKVKKNS DKDLGILICG TGVGVCMAAN KVKGVLAALV VSEKTAALAR QHDNANVLCL SSRFVTDSEN IKIVDDFLKA NFEGGRHQRR IDKIIRYEKE TE // ID RS13_MYCGE Reviewed; 124 AA. AC P47421; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2003, sequence version 2. DT 13-APR-2016, entry version 94. DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315}; GN Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; GN Synonyms=rps13 {ECO:0000255|HAMAP-Rule:MF_01315}; GN OrderedLocusNames=MG175; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-123. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71394.1; -; Genomic_DNA. DR EMBL; U01733; AAD10542.1; -; Genomic_DNA. DR PIR; D64219; D64219. DR RefSeq; WP_009885860.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47421; -. DR SMR; P47421; 2-120. DR STRING; 243273.MgenG_010200002279; -. DR EnsemblBacteria; AAC71394; AAC71394; MG_175. DR KEGG; mge:MG_175; -. DR PATRIC; 20009782; VBIMycGen98045_0197. DR eggNOG; ENOG4108Z04; Bacteria. DR eggNOG; COG0099; LUCA. DR KO; K02952; -. DR OMA; RTKNNSR; -. DR OrthoDB; EOG618R01; -. DR BioCyc; MGEN243273:GH2R-184-MONOMER; -. DR Proteomes; UP000000807; 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: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 1 124 30S ribosomal protein S13. FT /FTId=PRO_0000132108. SQ SEQUENCE 124 AA; 14051 MW; CDE655952AC3F8B0 CRC64; MARILGIDIP NQKRIEIALT YIFGIGLSSA KTILKKAKIN PDKRVKDLSE EELVAIRNAA SGYKIEGDLR REIALNIKHL TEIGSWKGIR HRKNLPVRGQ RTRTNARTRK GPRKTVANKK IESK // ID RS10_MYCGE Reviewed; 106 AA. AC P47396; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=30S ribosomal protein S10 {ECO:0000255|HAMAP-Rule:MF_00508}; GN Name=rpsJ {ECO:0000255|HAMAP-Rule:MF_00508}; GN Synonyms=rps10 {ECO:0000255|HAMAP-Rule:MF_00508}; GN OrderedLocusNames=MG150; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71368.1; -; Genomic_DNA. DR PIR; F64216; F64216. DR RefSeq; WP_009885835.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47396; -. DR STRING; 243273.MgenG_010200002134; -. DR EnsemblBacteria; AAC71368; AAC71368; MG_150. DR KEGG; mge:MG_150; -. DR PATRIC; 20009732; VBIMycGen98045_0172. DR eggNOG; ENOG4108Z10; Bacteria. DR eggNOG; COG0051; LUCA. DR KO; K02946; -. DR OMA; IESLMHI; -. DR OrthoDB; EOG6VXFHB; -. DR BioCyc; MGEN243273:GH2R-159-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. 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 1 106 30S ribosomal protein S10. FT /FTId=PRO_0000146552. SQ SEQUENCE 106 AA; 11961 MW; 91ADC496A978B19C CRC64; MNSAVKYPEL KIKLESYDST LLDLTIKKIV EVVKGVNIKI KGPLPLPTKK EVITIIRSPH VDKASREQFE KNTHKRLMIL VDVNQGGIDS LKKIKIPVGV TLRFSK // ID RS11_MYCGE Reviewed; 131 AA. AC P47422; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310}; GN Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; GN Synonyms=rps11 {ECO:0000255|HAMAP-Rule:MF_01310}; GN OrderedLocusNames=MG176; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71395.1; -; Genomic_DNA. DR EMBL; U01733; AAD10543.1; -; Genomic_DNA. DR PIR; E64219; E64219. DR ProteinModelPortal; P47422; -. DR STRING; 243273.MgenG_010200002284; -. DR EnsemblBacteria; AAC71395; AAC71395; MG_176. DR KEGG; mge:MG_176; -. DR PATRIC; 20009784; VBIMycGen98045_0198. DR eggNOG; ENOG4108UHH; Bacteria. DR eggNOG; COG0100; LUCA. DR KO; K02948; -. DR OrthoDB; EOG6ZSPF3; -. DR BioCyc; MGEN243273:GH2R-185-MONOMER; -. DR Proteomes; UP000000807; 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; 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 1 131 30S ribosomal protein S11. FT /FTId=PRO_0000123177. SQ SEQUENCE 131 AA; 14000 MW; DD3DE3F7F3FE48AD CRC64; MAKKKKINVP SGLIHVSCSP NNTIVSATDP SGNVLCWASS GTVGFKGFRK KTPYSAGVAA DKVAKTVKEM GMGSVKMYLK GTGRGKDTTI RSFANAGITI TEINEKTPIP HNGCKLLSVR ANQNNNLWKN F // ID RS12_MYCGE Reviewed; 139 AA. AC P47333; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. 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 Synonyms=rps12 {ECO:0000255|HAMAP-Rule:MF_00403}; GN OrderedLocusNames=MG087; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-139. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 -!- CAUTION: Because the enzyme that would modify Asp-102 to 3- CC methylthioaspartic acid has not been found in the proteome of this CC organism, that modification is not predicted. {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; L43967; AAC71305.1; -; Genomic_DNA. DR EMBL; U02212; AAD12506.1; -; Genomic_DNA. DR PIR; F64209; F64209. DR RefSeq; WP_010869326.1; NC_000908.2. DR ProteinModelPortal; P47333; -. DR SMR; P47333; 2-136. DR STRING; 243273.MgenG_010200000655; -. DR PRIDE; P47333; -. DR EnsemblBacteria; AAC71305; AAC71305; MG_087. DR KEGG; mge:MG_087; -. DR PATRIC; 20009576; VBIMycGen98045_0097. DR eggNOG; ENOG4108UKE; Bacteria. DR eggNOG; COG0048; LUCA. DR KO; K02950; -. DR OMA; LKSCPER; -. DR OrthoDB; EOG61ZTNF; -. DR BioCyc; MGEN243273:GH2R-90-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. 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; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 139 30S ribosomal protein S12. FT /FTId=PRO_0000146259. SQ SEQUENCE 139 AA; 15641 MW; CE6A4CF8C077ABDB CRC64; MATIAQLIRK PRQKKKVKSK SPALHYNLNL LNKKTTNVYS PLKRGVCTRV GTMTPRKPNS ALRKYAKVRL TNGFEVLAYI PGEGHNLQEH SVTLLRGGRV KDLPGVRYHI VRGTLDTVGV DKRRQQRSAY GAKKPKPKS // ID RS14Z_MYCGE Reviewed; 61 AA. AC P47410; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 85. 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=rps14 {ECO:0000255|HAMAP-Rule:MF_01364}, GN rpsN {ECO:0000255|HAMAP-Rule:MF_01364}; OrderedLocusNames=MG164; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71382.1; -; Genomic_DNA. DR PIR; B64218; B64218. DR RefSeq; WP_009885848.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47410; -. DR SMR; P47410; 2-61. DR STRING; 243273.MgenG_010200002209; -. DR EnsemblBacteria; AAC71382; AAC71382; MG_164. DR KEGG; mge:MG_164; -. DR PATRIC; 20009760; VBIMycGen98045_0186. DR eggNOG; ENOG41082QR; Bacteria. DR eggNOG; COG0199; LUCA. DR KO; K02954; -. DR OMA; RAYTRCN; -. DR OrthoDB; EOG6BCT0K; -. DR BioCyc; MGEN243273:GH2R-173-MONOMER; -. DR Proteomes; UP000000807; 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:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. 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_0000130906. 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; 6917 MW; 0B04CA96D071CD8F CRC64; MAKKSLKVKQ SRPNKFSVRD YTRCLRCGRA RAVLSHFGVC RLCFRELAYA GAIPGVKKAS W // ID RS16_MYCGE Reviewed; 89 AA. AC P47684; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 85. DE RecName: Full=30S ribosomal protein S16 {ECO:0000255|HAMAP-Rule:MF_00385}; GN Name=rpsP {ECO:0000255|HAMAP-Rule:MF_00385}; GN Synonyms=rps16 {ECO:0000255|HAMAP-Rule:MF_00385}; GN OrderedLocusNames=MG446; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC72466.1; -; Genomic_DNA. DR PIR; C64249; C64249. DR RefSeq; WP_014894702.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47684; -. DR STRING; 243273.MgenG_010200000220; -. DR EnsemblBacteria; AAC72466; AAC72466; MG_446. DR KEGG; mge:MG_446; -. DR PATRIC; 20010480; VBIMycGen98045_0513. DR eggNOG; ENOG4105K5M; Bacteria. DR eggNOG; COG0228; LUCA. DR KO; K02959; -. DR OMA; WKEFIAL; -. DR OrthoDB; EOG6CVVKH; -. DR BioCyc; MGEN243273:GH2R-499-MONOMER; -. DR Proteomes; UP000000807; 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; 3.30.1320.10; -; 1. DR HAMAP; MF_00385; Ribosomal_S16; 1. DR InterPro; IPR000307; Ribosomal_S16. 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. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 89 30S ribosomal protein S16. FT /FTId=PRO_0000167206. SQ SEQUENCE 89 AA; 10229 MW; C9A83AA1042289F1 CRC64; MRMGRVHYPL YRIVAVDSRV KRNGKYIALI GHLNPALKEN KCKLDETVAL DWLNKGAIPT DTVRSLFSES GLWKKFIESK NKKETSPKK // ID RS18_MYCGE Reviewed; 105 AA. AC P47338; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=30S ribosomal protein S18 {ECO:0000255|HAMAP-Rule:MF_00270}; GN Name=rpsR {ECO:0000255|HAMAP-Rule:MF_00270}; GN Synonyms=rps18 {ECO:0000255|HAMAP-Rule:MF_00270}; GN OrderedLocusNames=MG092; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71310.1; -; Genomic_DNA. DR PIR; B64210; B64210. DR ProteinModelPortal; P47338; -. DR STRING; 243273.MgenG_010200000685; -. DR EnsemblBacteria; AAC71310; AAC71310; MG_092. DR KEGG; mge:MG_092; -. DR PATRIC; 20009586; VBIMycGen98045_0102. DR eggNOG; ENOG4105VH8; Bacteria. DR eggNOG; COG0238; LUCA. DR KO; K02963; -. DR OMA; NQSEIRY; -. DR OrthoDB; EOG6PCQ4R; -. DR BioCyc; MGEN243273:GH2R-95-MONOMER; -. DR Proteomes; UP000000807; 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; 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 1 105 30S ribosomal protein S18. FT /FTId=PRO_0000111180. SQ SEQUENCE 105 AA; 12463 MW; 0D5F5A1276DF5A26 CRC64; MMINKEQDLN QLETNQEQSV EQNQTDEKRK PKPNFKRAKK YCRFCAIGQL RIDFIDDLEA IKRFLSPYAK INPRRITGNC NMHQRHVANA LKRARYLALV PFIKD // ID RS19_MYCGE Reviewed; 87 AA. AC P47401; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=30S ribosomal protein S19; GN Name=rpsS; Synonyms=rps19; OrderedLocusNames=MG155; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71373.1; -; Genomic_DNA. DR PIR; B64217; B64217. DR RefSeq; WP_009885839.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47401; -. DR SMR; P47401; 3-83. DR STRING; 243273.MgenG_010200002164; -. DR EnsemblBacteria; AAC71373; AAC71373; MG_155. DR KEGG; mge:MG_155; -. DR PATRIC; 20009742; VBIMycGen98045_0177. DR eggNOG; ENOG4105K7S; Bacteria. DR eggNOG; COG0185; LUCA. DR KO; K02965; -. DR OMA; VHNGRQF; -. DR OrthoDB; EOG61S365; -. DR BioCyc; MGEN243273:GH2R-164-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:InterPro. 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 87 30S ribosomal protein S19. FT /FTId=PRO_0000129860. SQ SEQUENCE 87 AA; 9997 MW; 0B8E6BED04CC47ED CRC64; MSRSSKKGAF VDAHLLKKVI EMNKQAKKKP IKTWSRRSTI FPEFVGNTFS VHNGKTFINV YVTDDMVGHK LGEFSPTRNF KQHTANR // ID RS4_MYCGE Reviewed; 205 AA. AC P47553; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306}; GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; GN Synonyms=rps4 {ECO:0000255|HAMAP-Rule:MF_01306}; GN OrderedLocusNames=MG311; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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:0000255|HAMAP-Rule:MF_01306}. CC -!- FUNCTION: With S5 and S12 plays an important role in translational CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}. 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. {ECO:0000255|HAMAP-Rule:MF_01306}. CC -!- SIMILARITY: Belongs to the ribosomal protein S4P family. CC {ECO:0000255|HAMAP-Rule:MF_01306}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_01306}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71533.1; -; Genomic_DNA. DR PIR; D64234; D64234. DR RefSeq; WP_009885889.1; NZ_AAGX01000008.1. DR ProteinModelPortal; P47553; -. DR STRING; 243273.MgenG_010200002544; -. DR EnsemblBacteria; AAC71533; AAC71533; MG_311. DR KEGG; mge:MG_311; -. DR PATRIC; 20010152; VBIMycGen98045_0362. DR eggNOG; ENOG4105G6W; Bacteria. DR eggNOG; COG0522; LUCA. DR KO; K02986; -. DR OMA; VESPRMA; -. DR OrthoDB; EOG6N3CXM; -. DR BioCyc; MGEN243273:GH2R-347-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:InterPro. 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; IPR018079; Ribosomal_S4_CS. 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; PS00632; RIBOSOMAL_S4; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 205 30S ribosomal protein S4. FT /FTId=PRO_0000132413. FT DOMAIN 95 158 S4 RNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_01306}. SQ SEQUENCE 205 AA; 23947 MW; 3F2861E791339118 CRC64; MKYTGSIFKR SRRLGFSLLE NNKEFSKGKK RKSIPGQHGN RFRSSTLSGY AQQLQEKQRM QYMYGITDKQ FRRLFRFVLK QKGNLTVNLF RVLESRLDNI VYRMGFAPTR KSARQMVNHG HVILNDQTVD TPSIIINPGD KVRLKARITK SPLVKNFIEN SVISSFVETN KKAFEGTYIR FPERSELPAG INESYVVEWY KRLVK // ID RRF_MYCGE Reviewed; 183 AA. AC P47673; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 90. 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=MG435; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC72456.1; -; Genomic_DNA. DR PIR; A64248; A64248. DR RefSeq; WP_010869481.1; NC_000908.2. DR ProteinModelPortal; P47673; -. DR STRING; 243273.MgenG_010200000285; -. DR EnsemblBacteria; AAC72456; AAC72456; MG_435. DR KEGG; mge:MG_435; -. DR PATRIC; 20010456; VBIMycGen98045_0501. DR eggNOG; ENOG4108VCV; Bacteria. DR eggNOG; COG0233; LUCA. DR KO; K02838; -. DR OMA; VQPWEKK; -. DR OrthoDB; EOG6SV5F9; -. DR BioCyc; MGEN243273:GH2R-489-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006415; P:translational termination; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1360.40; -; 1. DR HAMAP; MF_00040; RRF; 1. DR InterPro; IPR024946; Arg_repress_C-like. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 183 Ribosome-recycling factor. FT /FTId=PRO_0000167492. SQ SEQUENCE 183 AA; 21519 MW; 4D9B3104592EB1C0 CRC64; MTKAHYIDFF KQAADKKIQW LKEELTKIRT GRPNPKIFDN LLIESYGQKM PLISLAQVTI NPPREIIIKP FDPKSNTNAI YSEIQRANIG VQPVIDGEKI RVNFPQITQE TRLENIKHVK KIIEQIYQEL RVVRRDALQM IKKDNHNEDL ENSLKAEIEK INKNYSNQLE EIQKDKEKEL LTI // ID RS17_MYCGE Reviewed; 85 AA. AC P47406; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 85. DE RecName: Full=30S ribosomal protein S17 {ECO:0000255|HAMAP-Rule:MF_01345}; GN Name=rpsQ {ECO:0000255|HAMAP-Rule:MF_01345}; GN Synonyms=rps17 {ECO:0000255|HAMAP-Rule:MF_01345}; GN OrderedLocusNames=MG160; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71378.1; -; Genomic_DNA. DR PIR; G64217; G64217. DR RefSeq; WP_009885844.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47406; -. DR STRING; 243273.MgenG_010200002189; -. DR EnsemblBacteria; AAC71378; AAC71378; MG_160. DR KEGG; mge:MG_160; -. DR PATRIC; 20009752; VBIMycGen98045_0182. DR eggNOG; ENOG41082C5; Bacteria. DR eggNOG; COG0186; LUCA. DR KO; K02961; -. DR OMA; VEDHDYP; -. DR OrthoDB; EOG63JRH2; -. DR BioCyc; MGEN243273:GH2R-169-MONOMER; -. DR Proteomes; UP000000807; 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; 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 85 30S ribosomal protein S17. FT /FTId=PRO_0000128468. SQ SEQUENCE 85 AA; 9970 MW; CF4312108BB13EBE CRC64; MKRNQRKQLI GTVVSTKNAK TATVKVTSRF KHPLYHKSVI RHKKYHVHNF GELVANDGDR VQIIETRPLS ALKRWRIVKI IERAK // ID RS15_MYCGE Reviewed; 86 AA. AC P47663; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343}; GN Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; GN Synonyms=rps15 {ECO:0000255|HAMAP-Rule:MF_01343}; GN OrderedLocusNames=MG424; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71648.1; -; Genomic_DNA. DR PIR; H64246; H64246. DR RefSeq; WP_009885608.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47663; -. DR STRING; 243273.MgenG_010200000345; -. DR EnsemblBacteria; AAC71648; AAC71648; MG_424. DR KEGG; mge:MG_424; -. DR PATRIC; 20010434; VBIMycGen98045_0490. DR eggNOG; ENOG4105K77; Bacteria. DR eggNOG; COG0184; LUCA. DR KO; K02956; -. DR OMA; NEKDTGN; -. DR OrthoDB; EOG6B368J; -. DR BioCyc; MGEN243273:GH2R-478-MONOMER; -. DR Proteomes; UP000000807; 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 86 30S ribosomal protein S15. FT /FTId=PRO_0000115476. SQ SEQUENCE 86 AA; 10185 MW; 02EF8DAF4CE24BA1 CRC64; MKIDKEQIIK AHQLHKNDVG SVQVQISILT DQIKKLTDHL LANKKDFISK RGLYTKVSKR KRLLKYLKER NIETYRDLIK NLNLRG // ID RS20_MYCGE Reviewed; 88 AA. AC P55750; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 78. DE RecName: Full=30S ribosomal protein S20 {ECO:0000255|HAMAP-Rule:MF_00500}; GN Name=rpsT {ECO:0000255|HAMAP-Rule:MF_00500}; GN OrderedLocusNames=MG363.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RX PubMed=8638118; DOI=10.1126/science.271.5253.1302b; RA Robison K., Gilbert W., Church G.M.; RT "More Haemophilus and Mycoplasma genes."; RL Science 271:1302-1303(1996). 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; L43967; AAC71590.1; -; Genomic_DNA. DR RefSeq; WP_009885821.1; NZ_AAGX01000006.1. DR ProteinModelPortal; P55750; -. DR STRING; 243273.MgenG_010200001973; -. DR EnsemblBacteria; AAC71590; AAC71590; MG_522. DR KEGG; mge:MG_522; -. DR PATRIC; 20010308; VBIMycGen98045_0428. DR eggNOG; COG0268; LUCA. DR KO; K02968; -. DR OMA; NAVILHK; -. DR OrthoDB; EOG6HMXNQ; -. DR BioCyc; MGEN243273:GH2R-418-MONOMER; -. DR Proteomes; UP000000807; 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 88 30S ribosomal protein S20. FT /FTId=PRO_0000167990. SQ SEQUENCE 88 AA; 10105 MW; B75EC326490ECEC6 CRC64; MANIKSNEKR LRQDIKRNLN NKGQKTKLKT NVKKFNKEIN LDNLSSVYSQ ADRLARKGII SLNRAKRLKS KNAVILHKSN TNSTAKKQ // ID RS5_MYCGE Reviewed; 211 AA. AC P47414; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307}; GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; GN Synonyms=rps5 {ECO:0000255|HAMAP-Rule:MF_01307}; GN OrderedLocusNames=MG168; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 169-211. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71386.1; -; Genomic_DNA. DR EMBL; U01726; AAC43203.1; -; Unassigned_DNA. DR PIR; F64218; F64218. DR RefSeq; WP_009885854.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47414; -. DR STRING; 243273.MgenG_010200002239; -. DR EnsemblBacteria; AAC71386; AAC71386; MG_168. DR KEGG; mge:MG_168; -. DR PATRIC; 20009768; VBIMycGen98045_0190. DR eggNOG; ENOG4108RA9; Bacteria. DR eggNOG; COG0098; LUCA. DR KO; K02988; -. DR OMA; QNEGREG; -. DR OrthoDB; EOG6FJNM5; -. DR BioCyc; MGEN243273:GH2R-177-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:UniProtKB-HAMAP. 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 1 211 30S ribosomal protein S5. FT /FTId=PRO_0000131547. FT DOMAIN 58 121 S5 DRBM. {ECO:0000255|HAMAP- FT Rule:MF_01307}. SQ SEQUENCE 211 AA; 23188 MW; 235F18FCB4058E08 CRC64; MNDQKTTNTG LLTSTLKTKP KHNLKPSSEA IKKAVSKKEG HYKNKRFQKH NFNNKSEFEE RIVKLKRISK TTKGGRNMRF SVLVVVGNKK GKVGYGIAKA LEVPLAIKKA IKKAHNSIHT VEIHKGSIYH EVIGRKGASK VLLKPAPLGT GIIAGGAIRA IVELAGFSDI YTKNLGRNTP INMIHATMDG ILKQLSPKKV ALLRNKPISD L // ID RS9_MYCGE Reviewed; 132 AA. AC P47656; Q49447; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=30S ribosomal protein S9; GN Name=rpsI; Synonyms=rps9; OrderedLocusNames=MG417; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71643.1; -; Genomic_DNA. DR EMBL; U01744; AAD10556.1; -; Genomic_DNA. DR PIR; A64246; A64246. DR RefSeq; WP_010869475.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47656; -. DR STRING; 243273.MgenG_010200000400; -. DR EnsemblBacteria; AAC71643; AAC71643; MG_417. DR KEGG; mge:MG_417; -. DR PATRIC; 20010422; VBIMycGen98045_0484. DR eggNOG; ENOG4108UJD; Bacteria. DR eggNOG; COG0103; LUCA. DR KO; K02996; -. DR OMA; IKQGAAR; -. DR OrthoDB; EOG6MWNH0; -. DR BioCyc; MGEN243273:GH2R-472-MONOMER; -. DR Proteomes; UP000000807; 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; 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 1 132 30S ribosomal protein S9. FT /FTId=PRO_0000111375. FT CONFLICT 80 80 A -> R (in Ref. 2; AAD10556). FT {ECO:0000305}. SQ SEQUENCE 132 AA; 15148 MW; 958F84CF87F01043 CRC64; MDKKSFYGLG RRKSSTAKVY LYQSKDKGKI TINHRNPSDY FPNKLVIQDM EQPLELTKLK DNFDINVVVK GGGFTGQAGA IRLGIVRALI KFNPDLKKLL KTKKLTTRDK RAKERKKFGL YGARRAPQFT KR // ID RS21_MYCGE Reviewed; 62 AA. AC P57085; Q2MHS9; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 13-APR-2016, entry version 67. DE RecName: Full=30S ribosomal protein S21; GN Name=rpsU; OrderedLocusNames=MG210.2; ORFNames=MG_481; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ribosomal protein S21P 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; L43967; ABC59631.1; -; Genomic_DNA. DR RefSeq; WP_009885749.1; NZ_AAGX01000004.1. DR STRING; 243273.MgenG_010200001412; -. DR EnsemblBacteria; ABC59631; ABC59631; MG_481. DR KEGG; mge:MG_481; -. DR PATRIC; 20009878; VBIMycGen98045_0244. DR eggNOG; COG0828; LUCA. DR HOGENOM; HOG000154197; -. DR KO; K02970; -. DR OMA; KRTAMRY; -. DR OrthoDB; EOG6FBX3Z; -. DR BioCyc; MGEN243273:GH2R-221-MONOMER; -. DR Proteomes; UP000000807; 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_00358; Ribosomal_S21; 1. DR InterPro; IPR001911; Ribosomal_S21. DR Pfam; PF01165; Ribosomal_S21; 1. DR TIGRFAMs; TIGR00030; S21p; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 62 30S ribosomal protein S21. FT /FTId=PRO_0000178352. SQ SEQUENCE 62 AA; 7638 MW; 3983976B4F2CFE0E CRC64; MPKIEVKNDD LELALKKFKR ISLEVRRLAQ RHEYHLRKGM RLREKQKIAQ KKRRKFRSLA SH // ID RS3_MYCGE Reviewed; 268 AA. AC P47403; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 13-APR-2016, entry version 104. DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309}; GN Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; GN Synonyms=rps3 {ECO:0000255|HAMAP-Rule:MF_01309}; GN OrderedLocusNames=MG157; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71375.1; -; Genomic_DNA. DR PIR; D64217; D64217. DR RefSeq; WP_009885841.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47403; -. DR STRING; 243273.MgenG_010200002174; -. DR PRIDE; P47403; -. DR EnsemblBacteria; AAC71375; AAC71375; MG_157. DR KEGG; mge:MG_157; -. DR PATRIC; 20009746; VBIMycGen98045_0179. DR eggNOG; ENOG4105CKE; Bacteria. DR eggNOG; COG0092; LUCA. DR KO; K02982; -. DR OMA; KTNPIGN; -. DR OrthoDB; EOG6K13X3; -. DR BioCyc; MGEN243273:GH2R-166-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:InterPro. 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 268 30S ribosomal protein S3. FT /FTId=PRO_0000130150. FT DOMAIN 40 110 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_01309}. SQ SEQUENCE 268 AA; 29986 MW; 2BFE5D5D1923515E CRC64; MGQKVNSNGL RFGINKNWIS RWTASSNQQT ATWLVQDEKI RNLFFINYRN AQVSNVEIER TQTTVDVYVY AAQPALLIGS ENKNIQKITK MIQIIVGRKI KLDLTINEIG SPMLSSRIIA RDIANAIENR VPLRSAMRQA LTKVLKAGAN GIKVLVSGRL NGAEIARDKM YIEGNMPLST LRADIDYAFE KAKTTYGIIG VKVWINRGMI YAKGLNRTPA HILHPQKKQL KTPTIKKTNS VIAKQKLTGS DIETASLKAL TDNNQNHE // ID RS8_MYCGE Reviewed; 141 AA. AC P47411; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=30S ribosomal protein S8 {ECO:0000255|HAMAP-Rule:MF_01302}; GN Name=rpsH {ECO:0000255|HAMAP-Rule:MF_01302}; GN Synonyms=rps8 {ECO:0000255|HAMAP-Rule:MF_01302}; GN OrderedLocusNames=MG165; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71383.1; -; Genomic_DNA. DR PIR; C64218; C64218. DR RefSeq; WP_010869359.1; NC_000908.2. DR ProteinModelPortal; P47411; -. DR STRING; 243273.MgenG_010200002214; -. DR EnsemblBacteria; AAC71383; AAC71383; MG_165. DR KEGG; mge:MG_165; -. DR PATRIC; 20009762; VBIMycGen98045_0187. DR eggNOG; ENOG4108UJY; Bacteria. DR eggNOG; COG0096; LUCA. DR KO; K02994; -. DR OMA; RIYKNTR; -. DR OrthoDB; EOG6Z0QH1; -. DR BioCyc; MGEN243273:GH2R-174-MONOMER; -. DR Proteomes; UP000000807; 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_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 1 141 30S ribosomal protein S8. FT /FTId=PRO_0000126439. SQ SEQUENCE 141 AA; 15804 MW; DF1F2C983ECB07B2 CRC64; MIINKVPKAH FDPVSDLFTK INNARKAKLL TVTTIASKLK IAILEILIKE GYLANYQVLE NKTKTKKLVS FTLKYTQRRI CSINGVKQIS KPGLRIYRSF EKLPLVLNGL GIAIISTSDG VMTDKVARLK KIGGEILAYV W // ID RSMH_MYCGE Reviewed; 309 AA. AC P47464; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 92. 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=MG222; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71443.1; -; Genomic_DNA. DR PIR; E64224; E64224. DR RefSeq; WP_009885760.1; NZ_AAGX01000004.1. DR ProteinModelPortal; P47464; -. DR STRING; 243273.MgenG_010200001492; -. DR EnsemblBacteria; AAC71443; AAC71443; MG_222. DR KEGG; mge:MG_222; -. DR PATRIC; 20009924; VBIMycGen98045_0258. DR eggNOG; ENOG4105CGJ; Bacteria. DR eggNOG; COG0275; LUCA. DR KO; K03438; -. DR OMA; THIPRSR; -. DR OrthoDB; EOG6X9MQ1; -. DR BioCyc; MGEN243273:GH2R-244-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-HAMAP. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 309 Ribosomal RNA small subunit FT methyltransferase H. FT /FTId=PRO_0000108658. FT REGION 36 38 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 55 55 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 81 81 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01007}. FT BINDING 102 102 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 109 109 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. SQ SEQUENCE 309 AA; 35123 MW; 046AA5517780C606 CRC64; MLNNQQIHQS VLINEVIHNL NINPCGNYLD LTAGFAGHSQ KILEKLTTGT LTINDVDKES INFCQKLFFK NNNVVIIHDN FANFPVHLKQ LSITKFDGIL MDLGVSSHQL NQPNRGFSFK NDGPIDMRMD QSNQKNTALT VLKNLTEQKL SLILKKYGDI KHPKPIAIGL KKAVQTEKNL TTTQLAKVVK ECATGFEKYQ SRNYLAKVFQ AIRIYLNDEI TNLKTALTFI PNLLKNNSRF LVIVFHSIEE KIVRNFIAKL TSFIQPEALP IKLTPAYQLI TKKPILPSQK ELELNPRSRS AKLFVIQKN // ID RS2_MYCGE Reviewed; 284 AA. AC P47316; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=30S ribosomal protein S2; GN Name=rpsB; Synonyms=rps2; OrderedLocusNames=MG070; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71288.1; -; Genomic_DNA. DR PIR; G64207; G64207. DR RefSeq; WP_009885926.1; NZ_AAGX01000011.1. DR ProteinModelPortal; P47316; -. DR STRING; 243273.MgenG_010200002841; -. DR EnsemblBacteria; AAC71288; AAC71288; MG_070. DR KEGG; mge:MG_070; -. DR PATRIC; 20009542; VBIMycGen98045_0080. DR eggNOG; ENOG4105CE9; Bacteria. DR eggNOG; COG0052; LUCA. DR KO; K02967; -. DR OMA; RYIYCAR; -. DR OrthoDB; EOG6XWV6P; -. DR BioCyc; MGEN243273:GH2R-73-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. 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; PS00963; RIBOSOMAL_S2_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 284 30S ribosomal protein S2. FT /FTId=PRO_0000134197. SQ SEQUENCE 284 AA; 32747 MW; 0C81740DBC8552FF CRC64; MSDTNTEKPE LVSLNKLSEM RTNIGMVKRY WNPKMGFFIE PERKHNNDLL KLDLQYQALK TAYNFIKDVV KNHGQILFVG TKNDYVKKLV IDIAKRVNVA YITQRWLGGT LTNFKTLSIS INKLNKLVEQ QKQNANDLTK KENLLLSREI ERLEKFFGGV KNLKRLPNLI VIDDPVYEKN AVLEANSLKI PVVALCNTNT NPELVDFIIP ANNHQPQSTC LLMNLLADAI AEAKGFETLY AYKPDEQIQI EIPPKQERQV INRSNTRNIT NQRLNINRQQ QETL // ID RS7_MYCGE Reviewed; 155 AA. AC P47334; Q49326; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480}; GN Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480}; GN Synonyms=rps7 {ECO:0000255|HAMAP-Rule:MF_00480}; GN OrderedLocusNames=MG088; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 -!- SIMILARITY: Belongs to the ribosomal protein S7P family. CC {ECO:0000255|HAMAP-Rule:MF_00480}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD12505.1; 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; L43967; AAC71306.1; -; Genomic_DNA. DR EMBL; U02212; AAD12505.1; ALT_INIT; Genomic_DNA. DR PIR; G64209; G64209. DR RefSeq; WP_009885645.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47334; -. DR SMR; P47334; 9-147. DR STRING; 243273.MgenG_010200000660; -. DR EnsemblBacteria; AAC71306; AAC71306; MG_088. DR KEGG; mge:MG_088; -. DR PATRIC; 20009578; VBIMycGen98045_0098. DR eggNOG; ENOG4108UHY; Bacteria. DR eggNOG; COG0049; LUCA. DR KO; K02992; -. DR OMA; TKFVNHL; -. DR OrthoDB; EOG6P5ZKW; -. DR BioCyc; MGEN243273:GH2R-91-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 155 30S ribosomal protein S7. FT /FTId=PRO_0000124295. SQ SEQUENCE 155 AA; 17897 MW; C13965C38496DE69 CRC64; MRKNRALKRT VLPDPVFNNT LVTRIINVIM KDGKKGLAQR ILYGAFEIIE KRTNQQPLTV FEKAVDNVMP RLELKVRRIA GSNYQVPTEV PPDRRIALAL RWIVIFANKR NEKTMLERVA NEIIDAFNNT GASVKKKDDT HKMAEANKAF AHMRW // ID RSMI_MYCGE Reviewed; 277 AA. AC P47302; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 92. 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}; OrderedLocusNames=MG056; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71273.1; -; Genomic_DNA. DR PIR; B64206; B64206. DR RefSeq; WP_009885721.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47302; -. DR STRING; 243273.MgenG_010200001170; -. DR EnsemblBacteria; AAC71273; AAC71273; MG_056. DR KEGG; mge:MG_056; -. DR PATRIC; 20009494; VBIMycGen98045_0057. DR eggNOG; ENOG4107SPE; Bacteria. DR eggNOG; COG0313; LUCA. DR KO; K07056; -. DR OMA; KLHESHY; -. DR OrthoDB; EOG6677TH; -. DR BioCyc; MGEN243273:GH2R-58-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:UniProtKB-HAMAP. 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 1 277 Ribosomal RNA small subunit FT methyltransferase I. FT /FTId=PRO_0000211943. SQ SEQUENCE 277 AA; 31895 MW; CD25DD3930364B5C CRC64; MKTLKVVATP IGNIQEISER AKKALQDCEV LFCEDSRVTR KMLDLLNIDC KQKKFVINNS FKEKQNLTFA EEFITNFKCC LVSDAGYPSL SDPGNEMINW IISKNKEIRI EVINGPSALM CGLITSGFKT TPLLFLGFLS HKQNQLKNYL STYQNQKSTI VFFEAVHRLE NTLETVKNVF KNNDVFIGRE LTKLHESHYW FNTSENTLPD ITLKGEFVIV IDNQNINHQT LSSNQYLVYE IKKLMDIGVK LKDACNYLAK KMHLKSSMLY TLFHESI // ID RUVA_MYCGE Reviewed; 205 AA. AC Q49424; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 104. 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}; OrderedLocusNames=MG358; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC71583.1; 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; L43967; AAC71583.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_010869447.1; NC_000908.2. DR ProteinModelPortal; Q49424; -. DR PRIDE; Q49424; -. DR EnsemblBacteria; AAC71583; AAC71583; MG_358. DR KEGG; mge:MG_358; -. DR PATRIC; 20010296; VBIMycGen98045_0422. DR KO; K03550; -. DR OMA; IVEHNWI; -. DR OrthoDB; EOG679THG; -. DR BioCyc; MGEN243273:GH2R-412-MONOMER; -. DR Proteomes; UP000000807; 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 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; 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; SSF47781; SSF47781; 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 1 205 Holliday junction ATP-dependent DNA FT helicase RuvA. FT /FTId=PRO_0000094648. SQ SEQUENCE 205 AA; 23726 MW; 99E9D45DFBE37767 CRC64; MITSIFGKVT FVGKRKIIVE HNWISYWFNT KENHKFEKNL EKNKQIFCHI IKKIVANQII EEAFAFNTLE EKEWFCRLIE LNGIGSKTAL NLLNNDLEEI KQYILENNYS ALCGINGVNN KIARALLSLE IFEKSENNKN IKGVQVADGY DELFETLKSL GYKQQEIQDA LKMIEVKPDF DISQLVAEVI KLMSFKNNEI TNKTA // ID RUVB_MYCGE Reviewed; 307 AA. AC Q49425; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 101. 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}; OrderedLocusNames=MG359; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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. {ECO:0000255|HAMAP- CC Rule:MF_00016}. 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; L43967; AAC71584.1; -; Genomic_DNA. DR PIR; G64239; G64239. DR RefSeq; WP_009885816.1; NZ_AAGX01000006.1. DR ProteinModelPortal; Q49425; -. DR STRING; 243273.MgenG_010200001948; -. DR EnsemblBacteria; AAC71584; AAC71584; MG_359. DR KEGG; mge:MG_359; -. DR PATRIC; 20010298; VBIMycGen98045_0423. DR eggNOG; ENOG4105CKJ; Bacteria. DR eggNOG; COG2255; LUCA. DR KO; K03551; -. DR OMA; YEPYLMQ; -. DR OrthoDB; EOG6SR93S; -. DR BioCyc; MGEN243273:GH2R-413-MONOMER; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA recombination; KW DNA repair; Helicase; Hydrolase; Nucleotide-binding; KW Reference proteome; SOS response. FT CHAIN 1 307 Holliday junction ATP-dependent DNA FT helicase RuvB. FT /FTId=PRO_0000165556. FT NP_BIND 45 52 ATP. {ECO:0000255|HAMAP-Rule:MF_00016}. SQ SEQUENCE 307 AA; 35000 MW; 376E5138279E396C CRC64; MKLQIKPPNT FDEFVGKQEI ISQIQLSIKA SKLNKTQLDH ILLYGPPGVG KTTLARLIAN ELKTKLQIIQ GGHLQKPSDF LNAISLIKKG DVLFIDEIHA VAPNVMELMY PVMDVFKIQV LIGKDFNSKI VEMKVNPFTL IGATTQLGKI INPLEDRFGV ILNINYYSNA EIEKMVSIYG KQMKLELNSN EISAITEHSK QTPRIAIRIV RRIFEQKIVN KKIDLEGLFK NLMIYKNGLQ SIDVQYLEVL NRQNEPQGIK SISSMLGIDR HTIENKIEPF LLRENMIQKT KKGRIITNSG REYLVNF // ID RSGA_MYCGE Reviewed; 278 AA. AC P47356; Q49474; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 97. 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=engC; GN OrderedLocusNames=MG110; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-122. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 169-265. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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:0000255|HAMAP-Rule:MF_01820}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01820}; CC -!- SUBUNIT: Monomer. Associates with ribosomes. {ECO:0000255|HAMAP- CC Rule:MF_01820}. 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: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; L43967; AAC71328.1; -; Genomic_DNA. DR EMBL; X61518; CAB97510.1; -; Genomic_DNA. DR EMBL; U01714; AAC43187.1; -; Unassigned_DNA. DR RefSeq; WP_010869335.1; NC_000908.2. DR ProteinModelPortal; P47356; -. DR STRING; 243273.MgenG_010200000795; -. DR EnsemblBacteria; AAC71328; AAC71328; MG_110. DR KEGG; mge:MG_110; -. DR PATRIC; 20009624; VBIMycGen98045_0121. DR eggNOG; ENOG4105E06; Bacteria. DR eggNOG; COG1162; LUCA. DR KO; K06949; -. DR OMA; TKNEMAN; -. DR OrthoDB; EOG69SKDD; -. DR BioCyc; MGEN243273:GH2R-114-MONOMER; -. DR Proteomes; UP000000807; 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; 3.40.50.300; -; 1. DR HAMAP; MF_01820; GTPase_RsgA; 1. DR InterPro; IPR030378; G_CP_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA. DR InterPro; IPR010914; RsgA_GTPase_dom. DR Pfam; PF03193; DUF258; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00157; TIGR00157; 1. DR PROSITE; PS50936; ENGC_GTPASE; 1. DR PROSITE; PS51721; G_CP; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Hydrolase; Metal-binding; KW Nucleotide-binding; Reference proteome; Zinc. FT CHAIN 1 278 Putative ribosome biogenesis GTPase RsgA. FT /FTId=PRO_0000171494. FT DOMAIN 62 218 CP-type G. FT NP_BIND 112 115 GTP. {ECO:0000255|HAMAP-Rule:MF_01820}. FT NP_BIND 162 170 GTP. {ECO:0000255|HAMAP-Rule:MF_01820}. FT MOTIF 241 254 Knuckle-like cysteine cluster. FT METAL 241 241 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 246 246 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 248 248 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 254 254 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT CONFLICT 114 122 TDLDFDPME -> QTLILIQWK (in Ref. 3; FT CAB97510). {ECO:0000305}. SQ SEQUENCE 278 AA; 32147 MW; CE7C834E1B58ED9F CRC64; MPDSNFGIVL QSLAKQCKVF WNNQIITAFP QKKLQWKNDF KLMVGDRVQL EDGAITKVLA RKNELTRPRV ANVDQIVLIQ SLVQPKINWI QLLKLLVYFN AKLIDEIPIL ITKTDLDFDP MEKQKLIDLK QFNYQLFFVS KNEPLPSELI DIFSKKLSVF TGQSGVGKSS LINRLDPSLK QKIQALSVNK FGKNTTTKTT LFSFRGGFIC DTPGFNVISI KNLKILAAQH FVGFQKMISK CHFSNCYHQY EKDCFVTTSV MKNRYPSWLY EKYRKMIN // ID RS6_MYCGE Reviewed; 208 AA. AC P47336; Q49266; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=30S ribosomal protein S6; GN Name=rpsF; Synonyms=rps6; OrderedLocusNames=MG090; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 -!- SEQUENCE CAUTION: CC Sequence=AAD12413.1; 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; L43967; AAC71308.1; -; Genomic_DNA. DR EMBL; U02136; AAD12413.1; ALT_INIT; Genomic_DNA. DR PIR; I64209; I64209. DR RefSeq; WP_009885647.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47336; -. DR STRING; 243273.MgenG_010200000670; -. DR EnsemblBacteria; AAC71308; AAC71308; MG_090. DR KEGG; mge:MG_090; -. DR PATRIC; 20009582; VBIMycGen98045_0100. DR eggNOG; ENOG41068ZK; Bacteria. DR eggNOG; COG0360; LUCA. DR KO; K02990; -. DR OMA; RAANINK; -. DR OrthoDB; EOG6QK4TF; -. DR BioCyc; MGEN243273:GH2R-93-MONOMER; -. DR Proteomes; UP000000807; 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; 3.30.70.60; -; 1. DR HAMAP; MF_00360; Ribosomal_S6; 1. DR InterPro; IPR000529; Ribosomal_S6. DR InterPro; IPR020815; Ribosomal_S6_CS. 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. DR PROSITE; PS01048; RIBOSOMAL_S6; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 208 30S ribosomal protein S6. FT /FTId=PRO_0000176795. SQ SEQUENCE 208 AA; 24270 MW; E8095A612171C8F8 CRC64; MHYNIILLVD GTLSLEQANQ VEQKHQKLLE KATEFKSEYL GLKELAYPIK KQLSAHYYRW SFHGESNCTK EFKRAANINK QIIRELIINR EKDYGYLGSV NPKKQQLSLQ KLTKYNEIIA SENNPDNPDA PVTSGLASVK PRLSRVEKQK ERELEKWTVV HQSGNFDTVQ INPYRPRIKR FLQNNQQTSQ ANNNQPRFQN QFKKGAKP // ID RSMA_MYCGE Reviewed; 259 AA. AC P47701; Q49194; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 103. 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=MG463; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-248. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC72483.1; -; Genomic_DNA. DR EMBL; U01719; AAC43194.1; -; Unassigned_DNA. DR PIR; B64251; B64251. DR RefSeq; WP_010869490.1; NC_000908.2. DR ProteinModelPortal; P47701; -. DR EnsemblBacteria; AAC72483; AAC72483; MG_463. DR KEGG; mge:MG_463; -. DR PATRIC; 20010520; VBIMycGen98045_0533. DR KO; K02528; -. DR OMA; FGNIPYY; -. DR OrthoDB; EOG66F08Z; -. DR BioCyc; MGEN243273:GH2R-516-MONOMER; -. DR Proteomes; UP000000807; 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 1 259 Ribosomal RNA small subunit FT methyltransferase A. FT /FTId=PRO_0000101559. FT BINDING 13 13 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 15 15 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 40 40 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 61 61 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. FT BINDING 85 85 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. FT BINDING 105 105 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. FT CONFLICT 243 248 SPCQLF -> MSLSTL (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 259 AA; 29954 MW; DE67A0F2C28DACCA CRC64; MNSFFPSRKL GQNFTVNLSV IKRIFAFVKN LNPQAIVEIG VGKGALTNYL LKLKIPYKGI EIDKRLIEYL LVEKILTEDQ LVKGDILKKD FNSFFENLSP LLCGNIPYSI TSPIINKFLE SKLRSFVLMT QKEFANRLLA KVNSSDYSAF GAFCQYYLTI TTVFKIDRHA FKPKPKVDST LILLEKNKSV SYDFKFGLFL KQCFNQRRKM LINNLKHFFA VDYLLNIIQK QNLKTSIRAQ ELSPCQLFNL YQNICNGKN // ID RSMG_MYCGE Reviewed; 192 AA. AC P47620; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 87. 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}; OrderedLocusNames=MG380; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71607.1; -; Genomic_DNA. DR PIR; A64242; A64242. DR RefSeq; WP_009885942.1; NZ_AAGX01000012.1. DR ProteinModelPortal; P47620; -. DR STRING; 243273.MgenG_010200002956; -. DR PRIDE; P47620; -. DR EnsemblBacteria; AAC71607; AAC71607; MG_380. DR KEGG; mge:MG_380; -. DR PATRIC; 20010342; VBIMycGen98045_0445. DR eggNOG; COG0357; LUCA. DR KO; K03501; -. DR OrthoDB; EOG6HF639; -. DR BioCyc; MGEN243273:GH2R-435-MONOMER; -. DR Proteomes; UP000000807; 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 1 192 Ribosomal RNA small subunit FT methyltransferase G. FT /FTId=PRO_0000184286. FT REGION 111 112 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00074}. FT BINDING 59 59 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00074}. FT BINDING 124 124 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00074}. SQ SEQUENCE 192 AA; 22172 MW; 4440ECCD6204365C CRC64; MNNANFEKYV DLVFEANKNF NLTGFKTKEA IYQNLVIEIL TLFKGYEKFF IDKTVADLGS GNGSPGIILK LLFQKIKKLV LIDSKHKKIS FLNKLTKQLN LEKTVAICER IEVHKNHYDV ICSRGLSTII KVNDLAFSLL NSKGIIFHIK QSLDQYIEFE KSNQKNQFNL LFIKHFTSQN KKLILIALQK ND // ID SCPA_MYCGE Reviewed; 471 AA. AC P47455; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 81. DE RecName: Full=Segregation and condensation protein A; GN Name=scpA; OrderedLocusNames=MG213; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Participates in chromosomal partition during cell CC division. May act via the formation of a condensin-like complex CC containing Smc and ScpB that pull DNA away from mid-cell into both CC cell halves (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Component of a cohesin-like complex composed of ScpA, CC ScpB and the Smc homodimer, in which ScpA and ScpB bind to the CC head domain of Smc. The presence of the three proteins is required CC for the association of the complex with DNA (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associated CC with two foci at the outer edges of the nucleoid region in young CC cells, and at four foci within both cell halves in older cells. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ScpA 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; L43967; AAC71432.1; -; Genomic_DNA. DR PIR; E64223; E64223. DR RefSeq; WP_010869374.1; NC_000908.2. DR STRING; 243273.MgenG_010200001432; -. DR EnsemblBacteria; AAC71432; AAC71432; MG_213. DR KEGG; mge:MG_213; -. DR PATRIC; 20009886; VBIMycGen98045_0248. DR eggNOG; COG0262; LUCA. DR eggNOG; COG1354; LUCA. DR KO; K05896; -. DR OMA; DDELYIC; -. DR OrthoDB; EOG6X9MN8; -. DR BioCyc; MGEN243273:GH2R-225-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR InterPro; IPR003768; ScpA. DR Pfam; PF02616; SMC_ScpA; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Chromosome partition; Complete proteome; KW Cytoplasm; Reference proteome. FT CHAIN 1 471 Segregation and condensation protein A. FT /FTId=PRO_0000211094. FT REGION 143 471 ScpA. FT COMPBIAS 422 427 Poly-Gln. SQ SEQUENCE 471 AA; 54829 MW; 9531DEC11D790FE2 CRC64; MISLIFDKSN SFNPQLCVEL LNHFKVVMLT KTIVVDYPSF QAWKAQLKPF KLAVFSDNLQ TELTPNSKLT VFNNYQQLLV DNNDLIIFAT PTLVQLFDNE IDQLIVINPT SKSKDQFNCN WNDFVLIKQT NFKNHQVGYF DKKSSYEPPF TVVTDHFFGN LTDLFSLLVD KKVSVNDVDI GLISLQYLNI IANYTNKKAI EKITDYLVIT SKILAKKADN LLNDHQEESV LEYDLATNNF RDKMIANLVE HKRYCDSLGE FEKLRVNRLA YFSKANEMEQ FIKTANDQLV TVEDQLPNYI SVLKLFHAMN KLLEMRLSSL LTNKNITIKE LSVEQVQKEL VLAIKQFNYQ TVSLKRVLLK LNHPISLMYF VTAFVALLVL LNNQVIGLEQ KDYHSELYIF LLDENQLKTF QESPDEMVKR IQAQQQQNEL IIAKNKQLRA IKNKQKRADY LKKKYGENYL DKTNLKDENN N // ID SECG_MYCGE Reviewed; 77 AA. AC P58061; Q2MHT1; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 04-MAY-2001, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Probable protein-export membrane protein SecG; GN Name=secG; OrderedLocusNames=MG103.1; ORFNames=MG_476; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Medigue C., Bocs S.; RL Unpublished observations (MAY-2001). CC -!- FUNCTION: Involved in protein export. Participates in an early CC event of protein translocation (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the SecG 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; L43967; ABC59632.1; -; Genomic_DNA. DR RefSeq; WP_010869333.1; NZ_AAGX01000002.1. DR STRING; 243273.MgenG_010200000760; -. DR EnsemblBacteria; ABC59632; ABC59632; MG_476. DR KEGG; mge:MG_476; -. DR PATRIC; 20009610; VBIMycGen98045_0114. DR eggNOG; ENOG41074W1; Bacteria. DR eggNOG; COG1314; LUCA. DR HOGENOM; HOG000048765; -. DR KO; K03075; -. DR OMA; IVMFIMA; -. DR OrthoDB; EOG6DC6SJ; -. DR BioCyc; MGEN243273:GH2R-107-MONOMER; -. DR Proteomes; UP000000807; 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:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR004692; SecG. DR TIGRFAMs; TIGR00810; secG; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Protein transport; KW Reference proteome; Translocation; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 77 Probable protein-export membrane protein FT SecG. FT /FTId=PRO_0000157231. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 56 76 Helical. {ECO:0000255}. SQ SEQUENCE 77 AA; 8544 MW; F4AA12D8EDBB5C6D CRC64; MHPIQIVMFI MAVICLIIGL LLSNHGSTGG LASLSGQDLE IFRKTKDRGF VKILQIIMFI LVVLFLILGL IFSFAPR // ID SECA_MYCGE Reviewed; 806 AA. AC P47318; Q49438; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=MG072; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 494-702 AND 757-806. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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. Part of the essential Sec protein CC translocation apparatus which comprises SecA, SecYEG and auxiliary CC proteins SecDF. Other proteins may also be involved. CC {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- SUBCELLULAR LOCATION: Cell 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; L43967; AAC71290.1; -; Genomic_DNA. DR EMBL; U01732; AAD10541.1; -; Genomic_DNA. DR EMBL; U01743; AAD10553.1; -; Genomic_DNA. DR PIR; I64207; I64207. DR RefSeq; WP_009885928.1; NZ_AAGX01000011.1. DR ProteinModelPortal; P47318; -. DR SMR; P47318; 446-497. DR STRING; 243273.MgenG_010200002851; -. DR EnsemblBacteria; AAC71290; AAC71290; MG_072. DR KEGG; mge:MG_072; -. DR PATRIC; 20009546; VBIMycGen98045_0082. DR eggNOG; ENOG4105CI6; Bacteria. DR eggNOG; COG0653; LUCA. DR KO; K03070; -. DR OMA; EMGQVFN; -. DR OrthoDB; EOG654P48; -. DR BioCyc; MGEN243273:GH2R-75-MONOMER; -. DR Proteomes; UP000000807; 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; -; 3. DR Gene3D; 3.90.1440.10; -; 1. DR HAMAP; MF_01382; SecA; 1. 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; 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; 3. DR SUPFAM; SSF81767; SSF81767; 1. DR SUPFAM; SSF81886; SSF81886; 1. DR TIGRFAMs; TIGR00963; secA; 1. DR PROSITE; PS01312; SECA; 1. DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Membrane; KW Nucleotide-binding; Protein transport; Reference proteome; KW Translocation; Transport. FT CHAIN 1 806 Protein translocase subunit SecA. FT /FTId=PRO_0000109593. FT NP_BIND 102 109 ATP. {ECO:0000255|HAMAP-Rule:MF_01382}. FT CONFLICT 494 497 IRLG -> YPFS (in Ref. 2; AAD10541). FT {ECO:0000305}. FT CONFLICT 560 560 S -> T (in Ref. 2; AAD10541). FT {ECO:0000305}. FT CONFLICT 610 618 KQRDKFLLA -> TREVFIS (in Ref. 2; FT AAD10541). {ECO:0000305}. FT CONFLICT 624 625 MI -> WS (in Ref. 2; AAD10541). FT {ECO:0000305}. FT CONFLICT 629 629 L -> H (in Ref. 2; AAD10541). FT {ECO:0000305}. SQ SEQUENCE 806 AA; 91585 MW; FDD495AF98B1320F CRC64; MAIFNFLKLI SPKNRILSKA NRIASEVESY KNYYRNLTDQ QLFEESNKLV DLVTKQNYTI LDVCVAALAL IREVVYRETG EFAYRVQIIG AFIVLSGDFA EMMTGEGKTL TIVLAAYVSA LEKRGVHVVT VNEYLAQRDA NNAMKILKRV GMSVGCNFAN LSPQLKQAAF NCDVTYTTNS ELGFDYLRDN MVHSYQDKKI RELHFAIVDE GDSVLIDEAR TPLIISGPSK NEFGLYVAVD RFVKSLTEQE FKIDPESRAA SLTELGIKKA EQTFKKENLF ALENSDLFHK IMNGLTAVKV FEQGKEYIVR DGKVLIVDHF TGRILEGRSY SNGLQQAVQA KEYVEIEPEN VIVATITYQS FFRLYNRLAA VSGTALTESE EFLKIYNMVV VPVPTNRPNI RKDRSDSVFG TPQIKWMAVV KEIKKIHETS RPILIGTANI DDSELLHNLL LEANIPHEVL NAKNHSREAE IVTKAGQKNA VTISTNMAGR GTDIRLGEGV AEMGGLYVLG TERNESRRID NQLRGRAARQ GDKGETKFFI SLGDSLFKRF AHDKIERAIS KLGNETFDSA FFSKMLSRTQ KRVEAINFDT RKNLIDYDHV LASQRELIYK QRDKFLLAND LSEMIDKMLE KFVQQFCDQY RNQKNQNLIN HIALAEALNL EMNMQNTINP KVFENMTFDV AVDKTRNLVA KKISDKVNVL TKPIALNRFR DIIITSMDKH WTEHLDSVFK LREGVVLRSM EHTSPLNVYI KETDILFKTM LQKIAQDVIV QIANLTTPDE FDHSLMQANA LKKLAAIKAD EKSNQE // ID SCPB_MYCGE Reviewed; 207 AA. AC P47456; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Segregation and condensation protein B {ECO:0000255|HAMAP-Rule:MF_01804}; GN Name=scpB {ECO:0000255|HAMAP-Rule:MF_01804}; OrderedLocusNames=MG214; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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:0000255|HAMAP-Rule:MF_01804}. 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:0000255|HAMAP-Rule:MF_01804}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01804}. CC Note=Associated with two foci at the outer edges of the nucleoid CC region in young cells, and at four foci within both cell halves in CC older cells. {ECO:0000255|HAMAP-Rule:MF_01804}. CC -!- SIMILARITY: Belongs to the ScpB family. {ECO:0000255|HAMAP- CC Rule:MF_01804}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71433.1; -; Genomic_DNA. DR PIR; F64223; F64223. DR RefSeq; WP_009885754.1; NZ_AAGX01000004.1. DR ProteinModelPortal; P47456; -. DR STRING; 243273.MgenG_010200001437; -. DR EnsemblBacteria; AAC71433; AAC71433; MG_214. DR KEGG; mge:MG_214; -. DR PATRIC; 20009888; VBIMycGen98045_0249. DR eggNOG; ENOG4105K8I; Bacteria. DR eggNOG; COG1386; LUCA. DR KO; K06024; -. DR OMA; INVEINT; -. DR OrthoDB; EOG6CZQQQ; -. DR BioCyc; MGEN243273:GH2R-226-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 HAMAP; MF_01804; ScpB; 1. 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; Cell division; Chromosome partition; Complete proteome; KW Cytoplasm; Reference proteome. FT CHAIN 1 207 Segregation and condensation protein B. FT /FTId=PRO_0000211139. SQ SEQUENCE 207 AA; 23343 MW; 24741D38C557E56F CRC64; MKTTINIATP TLKKPSKEAN LVASIYGLLF VCGAKGITLR ELIRIFKKAG IEKVKLALLA LERKLADDEQ SGVELKKFGN SFSLVTKPII KDYLHLLLAH KVKNPLNSKA MEVLAIIAYN QPCTRPRINE IRGVDSFQIV DDLIAKELIV ELGRTDKPGR PFIYEVSAKF YDLFGIDSLD QLPKIEHFDL DKFKQGSFFD SNRYGDE // ID SECY_MYCGE Reviewed; 475 AA. AC P47416; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465}; GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=MG170; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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. {ECO:0000255|HAMAP- CC Rule:MF_01465}. 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:0000255|HAMAP-Rule:MF_01465}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01465}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01465}. CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. CC {ECO:0000255|HAMAP-Rule:MF_01465}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71388.1; -; Genomic_DNA. DR PIR; H64218; H64218. DR RefSeq; WP_009885855.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47416; -. DR STRING; 243273.MgenG_010200002254; -. DR EnsemblBacteria; AAC71388; AAC71388; MG_170. DR KEGG; mge:MG_170; -. DR PATRIC; 20009772; VBIMycGen98045_0192. DR eggNOG; ENOG4105CGG; Bacteria. DR eggNOG; COG0201; LUCA. DR KO; K03076; -. DR OMA; QTYVISQ; -. DR OrthoDB; EOG651SWP; -. DR BioCyc; MGEN243273:GH2R-179-MONOMER; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Protein transport; KW Reference proteome; Translocation; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 475 Protein translocase subunit SecY. FT /FTId=PRO_0000131735. FT TRANSMEM 26 46 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 65 87 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 128 148 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 163 183 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 194 214 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 232 252 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 284 304 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 325 345 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 385 405 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 411 431 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. SQ SEQUENCE 475 AA; 51845 MW; 073DAE0FC529DFAF CRC64; MQTVSSPKQK LNFGQRLLTL LQNRDFMVSL VLTVVLLILF RVLAIIPLPG IRINESVLDR NSNDFFSLFN LLGGGGLNQL SLFAVGISPY ISAQIIMQLL STDLIPPLSK LVNSGEVGRR KIEMITRIIT LPFALVQAFA VIQIATNAGT GSSPISLANS GSEFIAFYII AMTAGTYMAV FLGDTISKKG VGNGITLLIL SGILSQLPQG FIAAYNVLSG IVITLTPQLT AAISFFIYFL AFLVLLFATT FITQATRKIP IQQSGQGLVS EVKTLPYLPI KVNAAGVIPV IFASSIMSIP VTIAQFQPQT ESRWFVEDYL SLSTPVGIFL YAVLVILFSF FYSYIQINPE RLAKNFEKSG RFIPGIRPGN DTEKHIARVL IRINFIGAPF LTVIAIIPYI VSYFIRLPNS LSLGGTGIII IVTAVVEFIS ALRSAATATN YQQLRRNLAI EVQQTAKQDS LEQLQKEAPG IGNLW // ID SIGA_MYCGE Reviewed; 497 AA. AC P47491; Q49487; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 110. 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=MG249; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 222-323. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). 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 -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00963}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71469.1; -; Genomic_DNA. DR EMBL; X61535; CAB98133.1; -; Genomic_DNA. DR PIR; E64227; E64227. DR RefSeq; WP_009885787.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47491; -. DR SMR; P47491; 246-383. DR STRING; 243273.MgenG_010200001702; -. DR EnsemblBacteria; AAC71469; AAC71469; MG_249. DR KEGG; mge:MG_249; -. DR PATRIC; 20009980; VBIMycGen98045_0286. DR eggNOG; ENOG4105DG1; Bacteria. DR eggNOG; COG0568; LUCA. DR KO; K03086; -. DR OMA; YHEVLEA; -. DR OrthoDB; EOG6XHC70; -. DR BioCyc; MGEN243273:GH2R-271-MONOMER; -. DR Proteomes; UP000000807; 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; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR007624; RNA_pol_sigma70_r3. DR InterPro; IPR007630; RNA_pol_sigma70_r4. 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; 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome; KW Sigma factor; Transcription; Transcription regulation. FT CHAIN 1 497 RNA polymerase sigma factor SigA. FT /FTId=PRO_0000093899. FT DNA_BIND 451 470 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00963}. FT REGION 250 320 Sigma-70 factor domain-2. FT {ECO:0000255|HAMAP-Rule:MF_00963}. FT REGION 329 410 Sigma-70 factor domain-3. FT {ECO:0000255|HAMAP-Rule:MF_00963}. FT REGION 423 478 Sigma-70 factor domain-4. FT {ECO:0000255|HAMAP-Rule:MF_00963}. FT MOTIF 274 277 Interaction with polymerase core subunit FT RpoC. FT CONFLICT 224 232 DFESEQRIA -> NLNSGLP (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 497 AA; 57662 MW; ADE06CA668F59A65 CRC64; MSTDKKTLGE KPNSTKPELS EELIAELKKQ RILEKNRPYK KMIYVDNKVQ RKHRHENIAF LKTLHENKES DVPKKRRGRK PKHAPLKEKN NLKLFDILEG SLKSHIENDD TNTVINLLTE AWEKKSKKKQ KNITLSNKEI ISVLAKFELP EDEIIYVLDE LRDKGIQLQH DVEEHIHEFR ANQDLSIIDE DIEELTSKNI SNRDKVDDNV RFFLGSLDFS KMLDFESEQR IAKVLNSTDE ESRKYAINQL VTSNLRLVVS IAKKHLERGL DFNDLIQEGN LGLLKAISKF NWSLGNKFST YATWWIKQAI TRAIADQART VRIPVHMVET INRLAKAERA LYQELGREPT DEELAEKMGG QAEGFNVKKI AEIKRLSLDP VSLDKTVGHD EESQFGDFVK DTDAQTPDEF TESRSNSEKI DELLNNNLSE QEELIVRMRI GMPPYNEPKT LDEVGQKILI PREKIRQIEN KAIRKLRHAV RNNPISMSFL RINEKKD // ID SMC_MYCGE Reviewed; 982 AA. AC P47540; Q49301; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894}; DE AltName: Full=Protein P115 homolog; GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=MG298; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 915-981. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Required for chromosome condensation and partitioning. CC {ECO:0000255|HAMAP-Rule:MF_01894}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP- CC Rule:MF_01894}. CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|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; L43967; AAC71520.1; -; Genomic_DNA. DR EMBL; U02177; AAD12461.1; -; Genomic_DNA. DR PIR; I64232; I64232. DR RefSeq; WP_010869416.1; NC_000908.2. DR ProteinModelPortal; P47540; -. DR EnsemblBacteria; AAC71520; AAC71520; MG_298. DR KEGG; mge:MG_298; -. DR PATRIC; 20010126; VBIMycGen98045_0349. DR KO; K03529; -. DR OMA; THRQGTM; -. DR OrthoDB; EOG6WQD34; -. DR BioCyc; MGEN243273:GH2R-334-MONOMER; -. DR Proteomes; UP000000807; 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: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; -; 2. DR HAMAP; MF_01894; Smc_prok; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003395; RecF/RecN/SMC_N. DR InterPro; IPR010935; SMC_hinge. DR InterPro; IPR011890; SMC_prok. DR Pfam; PF06470; SMC_hinge; 1. DR Pfam; PF02463; SMC_N; 1. DR SMART; SM00968; SMC_hinge; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF75553; SSF75553; 1. PE 3: Inferred from homology; KW ATP-binding; Coiled coil; Complete proteome; Cytoplasm; DNA-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 982 Chromosome partition protein Smc. FT /FTId=PRO_0000119025. FT NP_BIND 33 40 ATP. {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 171 231 {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 280 310 {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 337 377 {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 575 718 {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 753 822 {ECO:0000255|HAMAP-Rule:MF_01894}. FT COMPBIAS 884 912 Ala/Asp-rich (DA-box). FT CONFLICT 975 982 YVSENDSN -> ICIWKWF (in Ref. 2; FT AAD12461). {ECO:0000305}. SQ SEQUENCE 982 AA; 111073 MW; E31CA2430B895A87 CRC64; MVFLKRFRAY GFKSYADEIT IDFTHSMTGI VGPNGSGKSN VVDALKWVLG ERSMKHLRSK SGDDMIFFGS KDKPASKLAE IELTFDNSNR LLHDSRKEIS VMRRVYRGSG QSEYFINSNP ATLKEISGIF ADIGLEKGSL GIISQGSVSW FVEAKPEERR KIFEDASGIG RYTKRKEEVV NQLNRTLINL KQVSVVLNEL KKDLKKLTLQ AEKAQQFIRV KNELKELELA VLVGEYLQAQ TELDKFNFQI NSSEHDFKIH EPQLELLEEQ IVIFNSRFHS ADMQSNELQK ELQDIYQKIN ELEQRKVIID VQLRQGFSQK DEKQKAAALK KLILVDQTQL DGFENQLSNS KTTITDLEKL INEQKSLVDQ IKLQIEKNTA DLIYQRSLKT IIELQTNELK KTNNANILVK NANALTGILN TLGTFLKFDK QYEKAILKAL GKSIGYLVVN NNNAAIQAID FLVKNEIGKV TFLPLDDVAS DTKITNEHME ILKQLDGFLG VCSDHVKCDP LFQPVVNTLL AQVIIAKDLN SAINLSNYTY KLYRIVTLDG ETVYAGGIIN GGFEKTNLSD GYLSSASLDN EQNINKLENN ERELKKELTE LEVKLDEMNR KLKYEELLQA KFIERIVQIK KIILELKMEY EQLTNTTFDG KKAVASEAEL IHSLNSAWAK RDEINSKLKL NQELKLQLAK TIKQSEEKIV DLRALLDEQR AKLVSAREGK IRFENTIQNI TEKINSVYKM TMEFAIANHN KPVKLSSMQA HNKIAKLQNQ LNEMGVINME SIAEISEKQK RFDDINAEYE SAQQAVENLQ KAITEIDEIA SNEFDQLIQK LNQELPKTFK YLFGGGSCQI RYTDPSNVLV SGIDVFANPP GKNIANLMLL SGGEKTLVAL SVLFSILKVS AFPLVILDEA ESALDPANVE RFANIIKTAS KNTQFLIITH RQGTMMKCDM LLGAAMQTKG VTKTFAVELE NAEKYVSEND SN // ID SPOT_MYCGE Reviewed; 720 AA. AC P47520; Q49221; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=Probable guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; DE EC=3.1.7.2; DE AltName: Full=Penta-phosphate guanosine-3'-pyrophosphohydrolase; DE Short=(ppGpp)ase; GN Name=spoT; OrderedLocusNames=MG278; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 131-224. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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. This enzyme catalyzes the CC degradation of ppGpp into GDP. It may also be capable of CC catalyzing the synthesis of ppGpp (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Guanosine 3',5'-bis(diphosphate) + H(2)O = CC guanosine 5'-diphosphate + diphosphate. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: CC step 1/1. CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HD 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; L43967; AAC71500.1; -; Genomic_DNA. DR EMBL; U01770; AAD10588.1; -; Genomic_DNA. DR PIR; G64230; G64230. DR RefSeq; WP_009885909.1; NZ_AAGX01000009.1. DR ProteinModelPortal; P47520; -. DR STRING; 243273.MgenG_010200002679; -. DR EnsemblBacteria; AAC71500; AAC71500; MG_278. DR KEGG; mge:MG_278; -. DR PATRIC; 20010056; VBIMycGen98045_0320. DR eggNOG; ENOG4105CWR; Bacteria. DR eggNOG; COG0317; LUCA. DR OMA; IIVENEF; -. DR OrthoDB; EOG6SV551; -. DR BioCyc; MGEN243273:GH2R-307-MONOMER; -. DR UniPathway; UPA00908; UER00886. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR004811; RelA/Spo_fam. DR InterPro; IPR007685; RelA_SpoT. DR Pfam; PF13328; HD_4; 1. DR Pfam; PF04607; RelA_SpoT; 1. DR SMART; SM00471; HDc; 1. DR SMART; SM00954; RelA_SpoT; 1. DR TIGRFAMs; TIGR00691; spoT_relA; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Manganese; Reference proteome. FT CHAIN 1 720 Probable guanosine-3',5'-bis(diphosphate) FT 3'-pyrophosphohydrolase. FT /FTId=PRO_0000166572. FT DOMAIN 49 154 HD. FT CONFLICT 219 224 YDNEWD -> LWQWVG (in Ref. 2; AAD10588). FT {ECO:0000305}. SQ SEQUENCE 720 AA; 84139 MW; 285A6E8670FD8A12 CRC64; MATIQEIECD FLAKIAQKFT NAEIELINKA FYHAKTWHEN QKRLSGEPFF IHPLRTALSL VEWNMDPITI CAGLLHDIIE DTDQTEANIA MIFSKEIAEL VTKVTKITNE SKKQRHLKNK KENLNLKSFV NIAINSQQEI NVMVLKLADR LDNIASIEFL PIEKQKVIAK ETLELYAKIA GRIGMYPVKT KLADLSFKVL DLKNYDNTLS KINKQKVFYD NEWDNFKQQL KKILAQNQIE YQLESRIKGI YSTYKKLTVH EQNISKIHDL FAIRLITKSE LDCYHILGLI HLNFLIDSKY FKDYIASPKQ NLYQSIHTTV RLKGLNVEIQ IRTQQMDNVS KFGLASHWIY KEQKEGLLAP ALQLNYLVTK QKHSHDFLKR IFGTDIIKIN VSASHEPNVI KQINVDSNNK LLDIAFENYP KQFAKLTKIE IDGVEINSFD TSVENEMLIE FYFGKNNNLK SKWIRYMNNP IYREKVKKSL AKLAKSGRYS ELAFYEKELG EKQLKLASET EIQKRLNTLR IKKMSDYLAL IECTNFTNDE HLLFLAKNND KWNKLTKPLK FAFSKVVFHN SYFEQIEGIF ITKIVIEPCC SKIPDMPEQV TGILTKNILS VHRYGCKNLQ NKKQLKIIPL YWNIQQLKLK PRKFRSYINI NGVWSEKTIN KICQTIINGD GYIEKIIPKI NKQKDEFDLN ITLFVNNYQQ LLTLMDQITT KNISFSWKYL // ID SRP54_MYCGE Reviewed; 446 AA. AC P47294; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Signal recognition particle protein {ECO:0000255|HAMAP-Rule:MF_00306}; DE AltName: Full=Fifty-four homolog {ECO:0000255|HAMAP-Rule:MF_00306}; GN Name=ffh {ECO:0000255|HAMAP-Rule:MF_00306}; OrderedLocusNames=MG048; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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:0000255|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:0000255|HAMAP-Rule:MF_00306}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00306}. CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. CC {ECO:0000255|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:0000255|HAMAP- CC Rule:MF_00306}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 CC subfamily. {ECO:0000255|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; L43967; AAC71264.1; -; Genomic_DNA. DR PIR; C64205; C64205. DR RefSeq; WP_010869306.1; NC_000908.2. DR ProteinModelPortal; P47294; -. DR STRING; 243273.MgenG_010200001110; -. DR EnsemblBacteria; AAC71264; AAC71264; MG_048. DR KEGG; mge:MG_048; -. DR PATRIC; 20009476; VBIMycGen98045_0048. DR eggNOG; ENOG4105CB9; Bacteria. DR eggNOG; COG0541; LUCA. DR KO; K03106; -. DR OMA; QFHPERI; -. DR OrthoDB; EOG62K1ZH; -. DR BioCyc; MGEN243273:GH2R-48-MONOMER; -. DR Proteomes; UP000000807; 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; Cytoplasm; GTP-binding; Nucleotide-binding; KW Reference proteome; Ribonucleoprotein; RNA-binding; KW Signal recognition particle. FT CHAIN 1 446 Signal recognition particle protein. FT /FTId=PRO_0000101159. FT NP_BIND 106 113 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT NP_BIND 188 192 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT NP_BIND 246 249 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. SQ SEQUENCE 446 AA; 50199 MW; 080F2255C8B5E5AE CRC64; MFKAMLSSIV MRTMQKKINA QTITEKDVEL VLKEIRIALL DADVNLLVVK NFIKAIRDKT VGQTIEPGQD LQKSLLKTIK TELINILSQP NQELNEKRPL KIMMVGLQGS GKTTTCGKLA YWLEKKYKQK TMLVGLDIYR PAAIEQLETL SQQTNSVFFA QGTQPVAKTT KAALSAFKTA KCQTIICDTA GRLQTNETLM DELVSVKNEL NPDEIIMVVD GLSGQEIINV AQTFHKRLKL TGFIISKLDS DARAGAALSL ASLLQVPIKL IGVSEKLDGL EQFHPERIAN RILGLGDVMS LVEKAEQVFD KKDLTKTISK MFLGKMDLED LLIYMQQMHK MGSVSSLIKM LPANFSVSEE NAELIENKIE LWKVLINSMT REERRHPKLI NRDPNRKQRI IKGSGRKMDE LNKLMKEWNK MQLKATEMGK LLKTGSNPFG GFGQFF // ID SSB_MYCGE Reviewed; 160 AA. AC P47337; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 85. DE RecName: Full=Single-stranded DNA-binding protein; DE Short=SSB; DE AltName: Full=Helix-destabilizing protein; GN Name=ssb; OrderedLocusNames=MG091; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 SSB domain. {ECO:0000255|PROSITE- CC ProRule:PRU00252}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71309.1; -; Genomic_DNA. DR PIR; A64210; A64210. DR RefSeq; WP_010869327.1; NC_000908.2. DR ProteinModelPortal; P47337; -. DR EnsemblBacteria; AAC71309; AAC71309; MG_091. DR KEGG; mge:MG_091; -. DR PATRIC; 20009584; VBIMycGen98045_0101. DR KO; K03111; -. DR OMA; PIFENDV; -. DR OrthoDB; EOG6M9F32; -. DR BioCyc; MGEN243273:GH2R-94-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000424; Primosome_PriB/ssb. DR InterPro; IPR011344; ssDNA-bd. DR Pfam; PF00436; SSB; 1. DR PIRSF; PIRSF002070; SSB; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS50935; SSB; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 160 Single-stranded DNA-binding protein. FT /FTId=PRO_0000096062. FT DOMAIN 1 99 SSB. {ECO:0000255|PROSITE- FT ProRule:PRU00252}. FT COMPBIAS 155 160 Asp/Glu-rich (acidic). SQ SEQUENCE 160 AA; 17973 MW; B1E78C759DC8BBE5 CRC64; MNRVFLFGKL SFTPNRLQTK NGTLGATFSM ECLDSSGFNN AKSFIRVTAW GKVASFIVAQ NPGVMLFVEG RLTTYKITNS ENKNTYALQV TADKIFHPDE KTTNEEPIKS TVVDSPFMNP KASVTEAEFE QAFPHQDETD FNNITPIFEN DVQLEEESDD // ID SSRP_MYCGE Reviewed; 145 AA. AC P47305; Q49505; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 95. 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}; OrderedLocusNames=MG059; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 83-145. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [3] RP DISRUPTION PHENOTYPE. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=10591650; DOI=10.1126/science.286.5447.2165; RA Hutchison C.A., Peterson S.N., Gill S.R., Cline R.T., White O., RA Fraser C.M., Smith H.O., Venter J.C.; RT "Global transposon mutagenesis and a minimal Mycoplasma genome."; RL Science 286:2165-2169(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 -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted. CC {ECO:0000269|PubMed:10591650}. CC -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000255|HAMAP- CC Rule:MF_00023}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71276.1; -; Genomic_DNA. DR EMBL; U01693; AAB01006.1; -; Genomic_DNA. DR PIR; E64206; E64206. DR RefSeq; WP_009885724.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47305; -. DR STRING; 243273.MgenG_010200001185; -. DR EnsemblBacteria; AAC71276; AAC71276; MG_059. DR KEGG; mge:MG_059; -. DR PATRIC; 20009500; VBIMycGen98045_0060. DR eggNOG; ENOG4108UH4; Bacteria. DR eggNOG; COG0691; LUCA. DR KO; K03664; -. DR OMA; FLLNAHI; -. DR OrthoDB; EOG6HXJ9P; -. DR BioCyc; MGEN243273:GH2R-61-MONOMER; -. DR Proteomes; UP000000807; 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 1 145 SsrA-binding protein. FT /FTId=PRO_0000102982. FT CONFLICT 83 85 KHE -> NMK (in Ref. 2; AAB01006). FT {ECO:0000305}. SQ SEQUENCE 145 AA; 16865 MW; 7F151AB68D454509 CRC64; MLILVNNPKA KYDYHLMESY CAGIVLKGSE VKALSLGQGS LKEAYVFVKN NELFLEQFTI PPYSFAGPLN HASDRIKKLL LNKHEIKQII NKKQQQSLSV IPSKVFFRNG KIKVEIWLAK PKKKFDKRET IKKKTIRREL EAEYR // ID SYA_MYCGE Reviewed; 900 AA. AC P47534; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 99. 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}; OrderedLocusNames=MG292; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71513.1; -; Genomic_DNA. DR PIR; C64232; C64232. DR RefSeq; WP_010869412.1; NC_000908.2. DR ProteinModelPortal; P47534; -. DR EnsemblBacteria; AAC71513; AAC71513; MG_292. DR KEGG; mge:MG_292; -. DR PATRIC; 20010114; VBIMycGen98045_0343. DR KO; K01872; -. DR OMA; LDVTHYK; -. DR OrthoDB; EOG6Q2SQ2; -. DR BioCyc; MGEN243273:GH2R-328-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. 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; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR012947; tRNA_SAD. 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 1 900 Alanine--tRNA ligase. FT /FTId=PRO_0000075149. FT METAL 568 568 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 572 572 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 672 672 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 676 676 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. SQ SEQUENCE 900 AA; 104302 MW; AA54520BFB3949A2 CRC64; MNWTTDKVRQ TWLDYFAKKD HLVLASKSLI PINDPSLLWI NSGVATLKDY FSARKTPPSK RLVNAQICLR VNDIENVGFT SRHQTLFEML GNFSIGDYFK TEAIDFAFDL LVNYYQLDPK RFYITVYEDD ETTYKRWIKH KIDKNHIIKC DKSRNFWDLG LGPCGPCTEI YYDRGEKFDP KKIGEKLFFE DIENDRYVEI WNIVFSQFNN DGNGNYTELA QKNIDTGAGI ERLVSVLQNS PTNFDTDIFL KLIKIIEAFC PFKYDPNSYF TFDPQKVKEQ SYFRIIADHF KAITFTISEG VLPGPNERNY VVRRLLRRAL IACKKLQLNL AFIEKIIDEI IASYENYYQH LKAKNETVKQ VVLKEINAFN KTIDLGLVLF EKSVKNNTLT PQLTFQLNET YGFPVEIIRE LVNQKGLTID WTVFDQLMAK HRSISKQNNQ TINFEKQNIN LVNFKTKSTF FYHKNKINAK VIGLFDENYL PVKELNNQSG YVVFDQTVLY ATSGGQRYDE GSCINHSNNN DQKISFQGVF KGPNKQHFHY FLVGSFKLND QVTLSHDETW RKLAANNHSL EHLLHAALQK EIDPLIKQSG AFKSAQKATI DFNLNRHLTR NELEKVENKI RSLIKQKISS KEIFTDFEGS QKLNAIAYFE EEYSQHEILR VIRFGDYSVE LCGGTHVANT ASIEDCFITD FYSLGAGRWR IEIISSNETI NNYLKAENQK LIQLKSELEK VLSLIDSSIF KVELKELQQR LDKFILPEKI TQLRDASDTL LALKNDINQL KTKNYKVSQQ ALALSIKKQL LSLVDENKSY VIATFNDVEP KLLLQTLHDV FNQNQTKNFL IINQFNESNS FIVIGNKTTT IIEKLRNSFN LKGGGNDKLF RGSFQDNVTP QKLNELFQNK // ID SYD_MYCGE Reviewed; 550 AA. AC P47282; Q49462; Q49479; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 118. DE RecName: Full=Aspartate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00044}; DE EC=6.1.1.12 {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}; GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; OrderedLocusNames=MG036; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 374-550. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-470. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Asp) in a CC two-step reaction: aspartate is first activated by ATP to form CC Asp-AMP and then transferred to the acceptor end of tRNA(Asp). CC {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP + CC diphosphate + L-aspartyl-tRNA(Asp). {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; L43967; AAC71252.1; -; Genomic_DNA. DR EMBL; U01814; AAD12351.1; -; Genomic_DNA. DR EMBL; X61523; CAA43736.1; -; Genomic_DNA. DR PIR; I64203; I64203. DR ProteinModelPortal; P47282; -. DR STRING; 243273.MgenG_010200001005; -. DR EnsemblBacteria; AAC71252; AAC71252; MG_036. DR KEGG; mge:MG_036; -. DR PATRIC; 20009448; VBIMycGen98045_0034. DR eggNOG; ENOG4105C9M; Bacteria. DR eggNOG; COG0173; LUCA. DR KO; K01876; -. DR OMA; SEEINQE; -. DR OrthoDB; EOG68Q0NX; -. DR BioCyc; MGEN243273:GH2R-36-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004815; F:aspartate-tRNA 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; 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; 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 1 550 Aspartate--tRNA ligase. FT /FTId=PRO_0000110902. FT NP_BIND 208 210 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT NP_BIND 499 502 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT REGION 186 189 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 162 162 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 208 208 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 217 217 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT BINDING 417 417 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 451 451 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT BINDING 454 454 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 458 458 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT CONFLICT 374 377 LGAI -> CWSN (in Ref. 2). {ECO:0000305}. FT CONFLICT 469 470 MN -> II (in Ref. 3). {ECO:0000305}. SQ SEQUENCE 550 AA; 64237 MW; 4B7972691E38D4BA CRC64; MCFNQRILIG SISTEQLNKT IVIIGWIKRI KKLGEINFII VGDKSGTIQV TCKDKEQIQQ LTREDIVIVK AKLQRLDSVR FELINPTIKL FSKSKTPPLI IEDETDALEE VRLKYRYLDL RRRLMQKRLL LRHQFILAIR NWFNQQGFIE IETPTLSKST PEGAQDFLVP ARIRKDCFYA LVQSPQIYKQ LLMIAGVEKY FQIARVYRDE DSRKDRQPEH TQIDFEISFC NQKMIMNLVE KLFFSVFLDV FQIKIKKTFP VFKFSELFER FGSDKPDLRY GFEIKDFTSL FQDHQNQFTK LIEAKGIIGG IELTNIELST DKIKALRKIA KDHDVSLEVH NKNNSTLKTS IKCDEKNTLL LVANKSKKKA WTALGAIRNE LKYHLDIVKP NQYSFCWVVD FPLYDFDEKT NQWISNHNIF SKPKQEWIDN FESNKNEALS EQFDLVLNGF EIGSGSIRIN DPIVQKRLMN SLNIDPNKFA FLLEAYQYGA PVHGGMGLGI DRLMMILNQT DNIREVIAFP KNNHGIEVHT NAPDKIDKEE VKWWIKELVK // ID SYH_MYCGE Reviewed; 414 AA. AC P47281; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 103. 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=MG035; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71251.1; -; Genomic_DNA. DR PIR; H64203; H64203. DR RefSeq; WP_009885699.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47281; -. DR STRING; 243273.MgenG_010200001000; -. DR EnsemblBacteria; AAC71251; AAC71251; MG_035. DR KEGG; mge:MG_035; -. DR PATRIC; 20009446; VBIMycGen98045_0033. DR eggNOG; ENOG4107R36; Bacteria. DR eggNOG; COG0124; LUCA. DR KO; K01892; -. DR OMA; YRQFWQF; -. DR OrthoDB; EOG6BPDH4; -. DR BioCyc; MGEN243273:GH2R-35-MONOMER; -. DR BRENDA; 6.1.1.21; 3528. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. 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 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 1 414 Histidine--tRNA ligase. FT /FTId=PRO_0000136198. SQ SEQUENCE 414 AA; 48324 MW; 9419FD5BDB12110A CRC64; MNFLQKPRGV KDWFGDELVY FNWIVKKIRS LAFNWGFSEV KTPLFENAQL FQRSNANADI VQKELYQFFD KSQRELALRP EATTPIVRLA CENKLMQEAN FPLKLFCIGS MYRYERPQNN RFREHWQFSC EVFGFSNLFI FLDTLLFANS LLEALGITGY VLKINNLANF ETLSKWNKAL KDYLTPYKLE LTELSQKRLE KNPLRILDDK IDQKKSFVKN APKITDFLDA SAKQDSELLK TQLKKHNISF EWTDNLVRGL DYYTGFVFEY VKNQDTILAG GVYDNLVEEL SSNPTPALGF ACGIERLINC LEIDKKAFIL NTKPKQMLVI CLFEEALEEL VWLAKLWREY NQVTIYPKVI KVDNGIRLAN RLGYTFIGIV GKTDFDKKAI TIKNLVSKQQ TIYTWNELGE RNVF // ID SYFA_MYCGE Reviewed; 341 AA. AC P47436; Q49515; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 103. 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=MG194; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-119 AND 232-335. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71412.1; -; Genomic_DNA. DR EMBL; U02120; AAD12394.1; -; Genomic_DNA. DR EMBL; U01711; AAB01023.1; -; Genomic_DNA. DR PIR; D64221; D64221. DR RefSeq; WP_010869368.1; NC_000908.2. DR ProteinModelPortal; P47436; -. DR EnsemblBacteria; AAC71412; AAC71412; MG_194. DR KEGG; mge:MG_194; -. DR PATRIC; 20009840; VBIMycGen98045_0226. DR KO; K01889; -. DR OrthoDB; EOG6WX4QN; -. DR BioCyc; MGEN243273:GH2R-202-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:InterPro. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. 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; IPR022911; Phe_tRNA_ligase_alpha1_bac. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR Pfam; PF01409; tRNA-synt_2d; 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 1 341 Phenylalanine--tRNA ligase alpha subunit. FT /FTId=PRO_0000126729. FT METAL 254 254 Magnesium. {ECO:0000250}. FT CONFLICT 232 238 MITHFFG -> YDHPFLW (in Ref. 2). FT {ECO:0000305}. FT CONFLICT 324 334 DIRDFYDNNFK -> VYLIFMITTLS (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 341 AA; 38982 MW; 1C6FAA7663C7A01D CRC64; MIDQNKLITK WKKAFAKAKN LTTLVNLKNT LHNSDLKPLL QKIKTATKLS EKSSLGKLYQ SLDIQLTDLL TSYKKTFEIN NQVSQKPSLD VMLPATEFTN GSNNALYQVI DNLVEYFKSF LFTINFDSEL TSISDCFDLL NIPKDHSSRN ESDSFYIDKT SLLRTHCTAT TLKAVRTSKK TNNPDIRVVS LGAVFRNDSD DATHSHQFTQ LDFMWIKKGL SLANLKWFIN NMITHFFGEN TFTRFRLSHF PFTEPSFEID IRCWLCQNGC SICKQTKWIE ILGAGIIHPQ VMNNMGIGDT ENITGIAAGI GIERLAMLKY GIDDIRDFYD NNFKFLTQFT D // ID SYG_MYCGE Reviewed; 446 AA. AC P47493; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 104. DE RecName: Full=Glycine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00253}; DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00253}; DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00253}; DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00253}; GN Name=glyQS {ECO:0000255|HAMAP-Rule:MF_00253}; Synonyms=glyS; GN OrderedLocusNames=MG251; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). CC {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71471.1; -; Genomic_DNA. DR PIR; G64227; G64227. DR RefSeq; WP_010869392.1; NC_000908.2. DR ProteinModelPortal; P47493; -. DR PRIDE; P47493; -. DR EnsemblBacteria; AAC71471; AAC71471; MG_251. DR KEGG; mge:MG_251; -. DR PATRIC; 20009984; VBIMycGen98045_0288. DR KO; K01880; -. DR OMA; RAAWDYG; -. DR OrthoDB; EOG6R87F8; -. DR BioCyc; MGEN243273:GH2R-273-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004820; F:glycine-tRNA ligase activity; ISS:UniProtKB. DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00253_B; Gly_tRNA_synth_B; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2. DR InterPro; IPR022961; Gly_tRNA_ligase_bac. DR InterPro; IPR002315; tRNA-synt_gly. DR PANTHER; PTHR10745; PTHR10745; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01043; TRNASYNTHGLY. DR SUPFAM; SSF52954; SSF52954; 1. DR TIGRFAMs; TIGR00389; glyS_dimeric; 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 1 446 Glycine--tRNA ligase. FT /FTId=PRO_0000072964. FT NP_BIND 190 192 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 200 205 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 275 276 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 319 322 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT REGION 205 209 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT REGION 315 319 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT BINDING 100 100 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT BINDING 158 158 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00253}. SQ SEQUENCE 446 AA; 52295 MW; 2BBA0ADCBF76E05A CRC64; MAKVYNQEVY VQFLKQHGFV FQSSEIYNGL NNSWDFGPLG AVLKQQIKQA LYNFFIKNKA DVLLVETPII LSELVWKASG HLANFVDTLV DCKSCKYRFR VDQINAEIKA KKDWNSFKVN CPNCHNQNWS EVRDFNLLFQ TEIGVVNNDK RLVFLRPETA QGSFINFKNI LQAKKRNLPF AIAQFGKSFR NEITPGNFLF RTREFEQFEI EWFCKPDDAN SLFEKQLIMV EQFLQTVLKI NPELLKKHEY DQSELAHYAK KTTDFLFNFP HGLKELWGLA NRGDFDLKQH QEFSKKSMSF FDSELNQHFL PFIIEPAVGI ERLFYALIVS SYRREIINEE EREVLSLPFD LCPEQIIVLP LVNKLKKEAF SVFETLAKTR WRVCFETTGS IGKRYRKADA IGIKYAVTFD FESLEDNAVT IRDRDTLVQQ RIAIKELPQW FMKNGQ // ID SYT_MYCGE Reviewed; 564 AA. AC P47615; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 109. 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=MG375; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 350-463. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71602.1; -; Genomic_DNA. DR EMBL; U02130; AAD12408.1; -; Genomic_DNA. DR PIR; E64241; E64241. DR RefSeq; WP_010869457.1; NC_000908.2. DR ProteinModelPortal; P47615; -. DR EnsemblBacteria; AAC71602; AAC71602; MG_375. DR KEGG; mge:MG_375; -. DR PATRIC; 20010332; VBIMycGen98045_0440. DR KO; K01868; -. DR OMA; ITIQLDM; -. DR OrthoDB; EOG61KBFJ; -. DR BioCyc; MGEN243273:GH2R-430-MONOMER; -. DR Proteomes; UP000000807; 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; 3.40.50.800; -; 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; IPR002320; Thr-tRNA-ligase_IIa. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01047; TRNASYNTHTHR. DR SUPFAM; SSF52954; SSF52954; 1. DR SUPFAM; SSF55186; SSF55186; 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 1 564 Threonine--tRNA ligase. FT /FTId=PRO_0000101007. FT REGION 167 464 Catalytic. FT METAL 260 260 Zinc; catalytic. {ECO:0000250}. FT METAL 311 311 Zinc; catalytic. {ECO:0000250}. FT METAL 441 441 Zinc; catalytic. {ECO:0000250}. SQ SEQUENCE 564 AA; 65596 MW; 2CA833DA7F7AC447 CRC64; MLAGVLLLQI WLKCKYANVQ FGEHGFNGDE FYLDFYINEN FSTKQFAKIE SDLNSLSSKL EGISQKFVSL DEALSFFEND QFTKNLLKKS NLNKFKITFF ENKHFWIEDL TLTFIKKSFI KLLNVSVNYF LGDPSQLQLQ RINGIFAQSK KELEQLIKEN EERLKKDHRS LGKQLELFSF DPLIGAGLPI WLAKGTTLRN IIGNFVHHQQ LLFGFNTVCS PVLANIELFK ISGHYQHYKE DMFPAIKLDS QAMMLRPMTC PHHCLIFKQK RYSYKKMPQR FSEDSILHRF EASGGLIGLE RVRCMTLLDN HIFCRADQIK SEIKNAFNLI QKVNKKFGFI FDRIDLSLHD PKNQSKFIDN PGLWRESESQ MENVLKDLNI QYQKEIGAAA FYGPKIDFQF KTIFKKMITI ATIQLDFLLP EKFDLTYIDK KNTLKKPVII HVGIIGTYER FIAALLEKTS GNFPLWLAPV QAVIIPVNIQ KHLKAAKKLY NKLLKENIRV NLDDNQDRLA KKVRQAIIEK IPLQLIVGDK EIENLEKLTC RGFKGEKITR ISFNNFVKRV RRDG // ID SYC_MYCGE Reviewed; 428 AA. AC P47495; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 111. 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=MG253; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71473.1; -; Genomic_DNA. DR PIR; I64227; I64227. DR ProteinModelPortal; P47495; -. DR EnsemblBacteria; AAC71473; AAC71473; MG_253. DR KEGG; mge:MG_253; -. DR PATRIC; 20009988; VBIMycGen98045_0290. DR KO; K01883; -. DR OMA; ENIQHYA; -. DR OrthoDB; EOG6RVFXC; -. DR BioCyc; MGEN243273:GH2R-275-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. 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 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 1 428 Cysteine--tRNA ligase. FT /FTId=PRO_0000159428. FT MOTIF 25 35 "HIGH" region. FT MOTIF 253 257 "KMSKS" region. FT METAL 23 23 Zinc. {ECO:0000250}. FT METAL 196 196 Zinc. {ECO:0000250}. FT METAL 221 221 Zinc. {ECO:0000250}. FT METAL 225 225 Zinc. {ECO:0000250}. FT BINDING 256 256 ATP. {ECO:0000250}. SQ SEQUENCE 428 AA; 49905 MW; 5E0F7C7418A5F32C CRC64; MIVDSVSQKP TTLVQKTINI YLCGPTVYND LHLGNTRPLI VFDVLNRVLK KAKYTVNFVQ NITDIDDKII KIAQQQEVSE SVVTKQQITA YKSLLKKLNI LPIKHIQITE KIDKIPDYID QLVNQNHAYV STQNNVYFAV NSLKQYGYLA NRMVHLEETD TDKKNKLDFV LWKITTAGIK WNSKWGLGRP GWHVECAFLI DYCFKNELTI HGGGVDLKFP HHENENALHM ALYNQPITKH WMHIGHLMIE NQKMSKSLQN FLLAVDFLNF HDFRVLRWIF YQKHYLHPID LNQSLIEKAN NDIQRIAKTL NVARTWLVYS EQSELISPKQ YDPVFSALLD NLNFANAVAA IWKLIKKINT SIKTKDFSVL REQLSFLEWS IDLLGISFKS IHTKLNVRLI KEWSILHKQK AMDKADQIRK KLIKKMLL // ID SYI_MYCGE Reviewed; 895 AA. AC P47587; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 114. 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}; OrderedLocusNames=MG345; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-371 AND 605-711. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71570.1; -; Genomic_DNA. DR EMBL; U02196; AAD12482.1; -; Genomic_DNA. DR EMBL; U02254; AAD12519.1; -; Genomic_DNA. DR PIR; B64238; B64238. DR ProteinModelPortal; P47587; -. DR STRING; 243273.MgenG_010200001853; -. DR EnsemblBacteria; AAC71570; AAC71570; MG_345. DR KEGG; mge:MG_345; -. DR PATRIC; 20010256; VBIMycGen98045_0405. DR eggNOG; COG0060; LUCA. DR KO; K01870; -. DR OrthoDB; EOG644ZM1; -. DR BioCyc; MGEN243273:GH2R-395-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:UniProtKB-HAMAP. 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 Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 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 1 895 Isoleucine--tRNA ligase. FT /FTId=PRO_0000098417. FT MOTIF 57 67 "HIGH" region. FT MOTIF 590 594 "KMSKS" region. FT METAL 869 869 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 872 872 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 888 888 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 891 891 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT BINDING 549 549 Aminoacyl-adenylate. {ECO:0000255|HAMAP- FT Rule:MF_02002}. FT BINDING 593 593 ATP. {ECO:0000255|HAMAP-Rule:MF_02002}. SQ SEQUENCE 895 AA; 104396 MW; 8C78DE6A05311B22 CRC64; MDLKKTLLMP KTSFAMQANL STSEKNFHDF WKDKKVFQKL KKQNKGKQIK ILHDGPPYAN GSIHVGHALN KILKDFILRS WLYEGYDVVF IPGWDCHGLP IEHAVSKKNP SSYSNLSTVE KRKLCHQFAL SQIAVQKEQF QRLGLLNDFQ NCYYTIDESF QFKELELFLQ AIKKGLIFQD LKPTYWSPIS RTSLAEAEIE YKEVNSIALY LTFKVSKSDF LDENANLLVW TTTPWTLPTN QAIAIHPDFD YLLFEYNQQK FVILEKLFEV FTNKLNWTNA IKLKKFKGSN LKNSSYSHCF YNKVLPVLMG IHVVDNEGTG IVHSSPAFGI DDFYLCQKNK IKEVLISIDE KGVFNNLLND KELENCFYLK ANDLIINRLK QNNSFIFSEV ISHREPHDWR SKTPVIYRAS KQLFIKTKSI KKQLKKQINQ VNFLNSKNQL RLKEMLLQRD EWCISRQRVW GLPIPIVYAN NKPLLDFSTI QYTIKQLKKH GIDSWFEKDV TCFLKPDKTK KWVKYHKEID TLDVWFDSGS SYNVLEINKY GSIADLYIEG SDQYRGWFNS SSNCGIIQND LIPFKSLVSH GFTLDENGNK MSKSLGNIVD PLKICDQYGA DILRLWVANT DWQIDNKIGV NILKQVAEQY RRIRNSLLRF ILGNINGFNF TSMDDYKFSL EDKIVIHKTN SLVEQIEKFL EKYNFLGCLK VINKFVLWLS SWYFEIIKDT LYCDAKNNPN RLAKQAVLNY IFTQLISFLN IFIPHTAEDA WKNYSFNKKP ISVNLFTKPT VFKVANSKNL GNIYKTFTSI KNAAFKEIEK LRKEGLISKN NQIELTVGIN KKIPKKLKDN LALWLNVNSV NLTNNENEIK VKKTKKTMCE RCWNFQTIIK QKLDHNLCSR CFKVC // ID SYN_MYCGE Reviewed; 456 AA. AC P47359; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=Asparagine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00534}; DE EC=6.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00534}; DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00534}; DE Short=AsnRS {ECO:0000255|HAMAP-Rule:MF_00534}; GN Name=asnS {ECO:0000255|HAMAP-Rule:MF_00534}; OrderedLocusNames=MG113; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 315-410. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP + CC diphosphate + L-asparaginyl-tRNA(Asn). {ECO:0000255|HAMAP- CC Rule:MF_00534}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00534}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00534}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00534}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71331.1; -; Genomic_DNA. DR EMBL; U01692; AAB01005.1; -; Genomic_DNA. DR PIR; E64212; E64212. DR RefSeq; WP_009885670.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47359; -. DR STRING; 243273.MgenG_010200000815; -. DR EnsemblBacteria; AAC71331; AAC71331; MG_113. DR KEGG; mge:MG_113; -. DR PATRIC; 20009630; VBIMycGen98045_0124. DR eggNOG; ENOG4105C5S; Bacteria. DR eggNOG; COG0017; LUCA. DR KO; K01893; -. DR OMA; WWYLDTR; -. DR OrthoDB; EOG6ZSP6X; -. DR BioCyc; MGEN243273:GH2R-117-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00534; Asn_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; IPR004522; Asn-tRNA-ligase. DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR PANTHER; PTHR22594; PTHR22594; 1. DR PANTHER; PTHR22594:SF6; PTHR22594:SF6; 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 TIGRFAMs; TIGR00457; asnS; 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 1 456 Asparagine--tRNA ligase. FT /FTId=PRO_0000176428. SQ SEQUENCE 456 AA; 52086 MW; 3E618BE362005FB9 CRC64; MKSVTVKQLL QTPRKFNNKQ IKLSGWVKNK RASANIIFLA ISDGSSINTL QAVVKQEDNP QVFSLLQTVN LASAVMVWGE IILTPKAKQP LELKLKQVSL LAQAESDYPL QKKEHSQEFF RSNAHLRVRA KTYFAVMKIR SVLSHAIFEY FFKNDFILVQ SPILTSNDCE GAGETFVIKD SETFFNKTTF LTVSGQFGAE AFAQAFKKVF TFGPTFRAEK SHTNRHLSEF WMIEPEIAFA NLKDLMQLIQ NLIKFLIKKV MENASDELNV LAKQFSNDII SNLKTIISTK KFPIIEYSKA LAILKESSDT KKTNFELNDF SFGIDLKTEH ERFLCEQYFQ NQPLFVINYP KELKAFYMKT NTDNKTVAAV DLLLPKIGEI CGGSERESDL NQLKNRCQSL NIDTKSLNWY LDMRKWGYFA SAGFGLGFDR LLAYICGLEN IRDAIPFPRV HGTINF // ID SYP_MYCGE Reviewed; 483 AA. AC P47525; Q49322; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 107. DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01571}; DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01571}; DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01571}; DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01571}; GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01571}; OrderedLocusNames=MG283; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-367. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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). CC {ECO:0000255|HAMAP-Rule:MF_01571}. CC -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP + CC diphosphate + L-prolyl-tRNA(Pro). {ECO:0000255|HAMAP- CC Rule:MF_01571}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01571}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01571}. CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic CC domain, the anticodon-binding domain and the C-terminal extension. CC {ECO:0000255|HAMAP-Rule:MF_01571}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. ProS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_01571}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71505.1; -; Genomic_DNA. DR EMBL; U02205; AAD12494.1; -; Genomic_DNA. DR PIR; C64231; C64231. DR RefSeq; WP_009885995.1; NZ_AAGX01000018.1. DR ProteinModelPortal; P47525; -. DR STRING; 243273.MgenG_010200003285; -. DR EnsemblBacteria; AAC71505; AAC71505; MG_283. DR KEGG; mge:MG_283; -. DR PATRIC; 20010078; VBIMycGen98045_0326. DR eggNOG; ENOG4107R1M; Bacteria. DR eggNOG; COG0442; LUCA. DR KO; K01881; -. DR OMA; RNITPRE; -. DR OrthoDB; EOG6G7R2R; -. DR BioCyc; MGEN243273:GH2R-317-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; 3.30.110.30; -; 1. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_01571; Pro_tRNA_synth_type3; 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; IPR004499; Pro-tRNA-ligase_IIa_arc-type. DR InterPro; IPR016061; Pro-tRNA_ligase_II_C. DR InterPro; IPR017449; Pro-tRNA_synth_II. DR PANTHER; PTHR11451:SF6; PTHR11451:SF6; 2. DR Pfam; PF09180; ProRS-C_1; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01046; TRNASYNTHPRO. DR SMART; SM00946; ProRS-C_1; 1. DR SUPFAM; SSF52954; SSF52954; 1. DR SUPFAM; SSF64586; SSF64586; 1. DR TIGRFAMs; TIGR00408; proS_fam_I; 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 1 483 Proline--tRNA ligase. FT /FTId=PRO_0000139333. FT CONFLICT 367 367 I -> Y (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 483 AA; 55869 MW; 7CD86861298C3343 CRC64; MTKKTQDLTS WYDQLLVKAK LICHGEVKGT VCFLNNSWGL WMEIQQLYND AIANKNQLSA IALTKFQPTT SFCYQVFQVQ LPTLSFYSEY QKEKTHIKGF NPELFLINQV GQKQLNDPLV LRPTSEIAFC NLWKKQELSY HDLPLIYNQW TQVFRAEKNT RPFLRNSEFY WQETHGLFVD QSQSEQAAIS FWNLYQDLII NKLCIPAFVG LKSESEKFAG AKNTWTIEAI MPDGQSLQCA TSHDLGDTFT KSFTISYQSK TNQKMTPSSF SCGMSTRILG AIFLTHSDDY GLVLPWYLAS KQVKLYLFDK NNNPKTRALA FLVKDFLEKL KIRFSFIEIN NQLGKQLLKG EIEGIPLQMI VDNEKTINIF NRLTRLKTSL TFANLQTEFV NLVNNYHTEM YRKANDLVEQ KLARVQTLKE IEQAFKNKKA VLCTVKLTGE LEQHLKTKYQ VSVRCVFKKS DVTQNCPFTN QPCFDSVLIA RAY // ID SYE_MYCGE Reviewed; 484 AA. AC P47700; Q49256; Q49306; Q49490; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00022}; DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022}; DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00022}; DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_00022}; GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_00022}; OrderedLocusNames=MG462; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 188-236. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-151 AND 362-484. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC72482.1; -; Genomic_DNA. DR EMBL; X61538; CAA43750.1; -; Genomic_DNA. DR EMBL; U02183; AAD12469.1; -; Genomic_DNA. DR EMBL; U02122; AAD12397.1; -; Genomic_DNA. DR PIR; A64251; A64251. DR RefSeq; WP_009885570.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47700; -. DR STRING; 243273.MgenG_010200000110; -. DR EnsemblBacteria; AAC72482; AAC72482; MG_462. DR KEGG; mge:MG_462; -. DR PATRIC; 20010518; VBIMycGen98045_0532. DR eggNOG; ENOG4105C20; Bacteria. DR eggNOG; COG0008; LUCA. DR KO; K01885; -. DR OMA; QLCYMPL; -. DR OrthoDB; EOG6DRPF7; -. DR BioCyc; MGEN243273:GH2R-515-MONOMER; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 484 Glutamate--tRNA ligase. FT /FTId=PRO_0000119601. FT MOTIF 10 20 "HIGH" region. FT MOTIF 252 256 "KMSKS" region. FT BINDING 255 255 ATP. {ECO:0000255|HAMAP-Rule:MF_00022}. FT CONFLICT 60 60 D -> EL (in Ref. 3; AAD12469). FT {ECO:0000305}. FT CONFLICT 230 230 A -> V (in Ref. 2). {ECO:0000305}. FT CONFLICT 362 362 L -> T (in Ref. 3). {ECO:0000305}. SQ SEQUENCE 484 AA; 55941 MW; B1E81B3839A45F6D CRC64; MEKIRTRYAP SPTGYLHVGG TRTAIFNFLL AKHFNGEFII RIEDTDTERN IKEGINSQFD NLRWLGVIAD ESVYNPGNYG PYLQSQKLAV YKKLAFDLIE KNLAYRCFCS KEKLESDRKQ AINNHKTPKY LGHCRNLHSK KITNHLEKND PFTIRLKINN EAEYSWNDLV RGQITIPGSA LTDIVILKAN GVATYNFAVV IDDYDMEITD VLRGAEHISN TAYQLAIYQA LGFKRIPRFG HLSVIVDESG KKLSKRDEKT TQFIEQFKQQ GYLPEALLNF LALLGWHPQY NQEFFNLKQL IENFSLSRVV SAPAFFDIKK LQWINANYIK QLTDNAYFNF IDNYLDVKVD YLKDKNREIS LLFKNQITHG VQINELIRES FATKIGVENL AKKSHILFKN IKLFLEQLAK SLQGLEEWKA EQIKTTINKV GAVFNLKGKQ LFMPIRLIFT NKEHGPDLAH IIEIFDKESA INLIKQFINA TNLF // ID SYFB_MYCGE Reviewed; 806 AA. AC P47437; Q49516; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 108. 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=MG195; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94 AND 682-798. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 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; L43967; AAC71413.1; -; Genomic_DNA. DR EMBL; U01711; AAB01024.1; -; Genomic_DNA. DR EMBL; U02173; AAD12455.1; -; Genomic_DNA. DR PIR; E64221; E64221. DR RefSeq; WP_009885736.1; NZ_AAGX01000004.1. DR ProteinModelPortal; P47437; -. DR STRING; 243273.MgenG_010200001307; -. DR EnsemblBacteria; AAC71413; AAC71413; MG_195. DR KEGG; mge:MG_195; -. DR PATRIC; 20009842; VBIMycGen98045_0227. DR eggNOG; ENOG4108H05; Bacteria. DR eggNOG; COG0072; LUCA. DR eggNOG; COG0073; LUCA. DR KO; K01890; -. DR OMA; YFRFYGY; -. DR OrthoDB; EOG6CCH1J; -. DR BioCyc; MGEN243273:GH2R-203-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.56.20; -; 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; IPR002547; tRNA-bd_dom. DR InterPro; IPR005147; tRNA_synthase_B5-dom. DR Pfam; PF03483; B3_4; 1. DR Pfam; PF03484; B5; 1. DR Pfam; PF01588; tRNA_bind; 1. DR SMART; SM00873; B3_4; 1. DR SMART; SM00874; B5; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF56037; SSF56037; 1. DR TIGRFAMs; TIGR00472; pheT_bact; 1. DR PROSITE; PS51483; B5; 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 1 806 Phenylalanine--tRNA ligase beta subunit. FT /FTId=PRO_0000126912. FT DOMAIN 40 153 tRNA-binding. FT DOMAIN 413 487 B5. FT METAL 465 465 Magnesium. {ECO:0000250}. FT METAL 471 471 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 474 474 Magnesium. {ECO:0000250}. FT METAL 475 475 Magnesium. {ECO:0000250}. FT CONFLICT 81 94 NANNINNPDNINKF -> MLITLTILYIHSCL (in Ref. FT 2). {ECO:0000305}. SQ SEQUENCE 806 AA; 92133 MW; D2F2BA6E9A064478 CRC64; MLISKKTLGV LIPDIFSFSN DQIAQKLEQM GIEVESIKQF NSPDYLQLAK VVSIQPHPHD NKLFICELQI DKNKFINVVS NANNINNPDN INKFVIVAKK GTELLNGLIV KTQNIKGIIS EGILCSYIDI NPFSRQIIEK TEVADAIIID HVSNDHDWNQ YLSFLSLDDV IFDVKTPTNR ADLHSLIFLA KELGVLLKTK TFLKQKSSVV NHDFFKFPLN LKNKLKANYF GGLFLRQINQ HSSPWTVKGL LINQMIKPVN YYVDKANLVT VFTAQPIHCH DADRIVGNIE LKQATHNETF VGLDDKQYEI EPGDIVVCDE KGIIALVGII GSKRTMVQPT TTNIFFEVVN CNSETIKQTA KRFLINNFAS KFMVKPISLL ATDNCLNYLQ NSLLTTDNIG KISHFSSSLK VEPFSKKLTV NFHKIRQLIG IEKKELTDQT IKKSLSQLGF KVDNQLLKIP SYRQDINTWQ DISEEIVKLI DINKLKPIGI TSSFNFEKSS YFNTFNALTK LRKKLQTLGF HNVITYQLTD QKSAKTFNLF NLENFITIKN PVSQNHSVMR VSLIDSLLKV LKTNNNYKNE LVNIFEFSFI KTQNNSELHL AVLWVEKLFT SSFNPMQGIS NDVFTMKGLA KLIVANLGFS CDFEPLDDSD YFVNNQSLKI VVFNEQIGFI GLIKESLLNN YDLNNKPIYC LEINLDRMLS SLNRIEKNYL GYSKLQPVCK DLTFSFTNPA SHFDQFANMI KRITGIESWK LISVFETMQN NQLITKYTVR YFLKNDANKP LTNQTIELIT NNLKLQCEKL KIKLDI // ID SYK_MYCGE Reviewed; 490 AA. AC P47382; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 113. 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=MG136; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71353.1; -; Genomic_DNA. DR PIR; A64215; A64215. DR RefSeq; WP_009885692.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47382; -. DR STRING; 243273.MgenG_010200000955; -. DR EnsemblBacteria; AAC71353; AAC71353; MG_136. DR KEGG; mge:MG_136; -. DR PATRIC; 20009678; VBIMycGen98045_0148. DR eggNOG; ENOG4105CRK; Bacteria. DR eggNOG; COG1190; LUCA. DR KO; K04567; -. DR OMA; DMMNLTE; -. DR OrthoDB; EOG69PQ2M; -. DR BioCyc; MGEN243273:GH2R-140-MONOMER; -. DR Proteomes; UP000000807; 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 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 1 490 Lysine--tRNA ligase. FT /FTId=PRO_0000152646. FT METAL 400 400 Magnesium 1. {ECO:0000250}. FT METAL 407 407 Magnesium 1. {ECO:0000250}. FT METAL 407 407 Magnesium 2. {ECO:0000250}. SQ SEQUENCE 490 AA; 56565 MW; 7F0BB0D76A0C13C6 CRC64; MSDRLNDQAQ HRLQKLLRLK QTNNDPYLVT KTSLTHSSKS FQVEFEKCSE EELKKKATVS LAGRIIAIRQ TFLIIQDFDG QVQLYINKKI HPKLFDYFNE FVDIGDQIVV SGKPMLTKTK VLTLAVEEMK IIAKCLLVPP EKWHGLTDIE TRARKRFLDL TYNLAMRDVF LKRTKIIKSI RSFLDQNGFI EVETPTLQAV LGGANAKPFK THYNALKADF YLRIANEIAL KKLIIGGFNK VYEMGKMFRN EGVDTTHNPE FTSIEIYQAY ADFEVMLVLV EKLIQSLCES LNQFSFNWNN KTINLKTPFH KITMVELIKK VTGIDFNSVK DDQSAILLAE KHHVKLAKHQ QNKQHIINLF FEQFCEQTLI EPTFVTHYPK AVSPLAKQDP SNPEFTQRFE LFINGKEIAN AYSELNDPLE QRKRFEQQLE EKQLGNDETS ELDESFLEAL SFGMVNTAGL GIGIDRLVML LCECNSIRDV VFFPQLREHK // ID SYL_MYCGE Reviewed; 792 AA. AC P47508; Q49228; Q49290; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 108. 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}; OrderedLocusNames=MG266; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-96 AND 208-319. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71488.1; -; Genomic_DNA. DR EMBL; U01780; AAD10600.1; -; Genomic_DNA. DR EMBL; U02167; AAD12449.1; -; Genomic_DNA. DR PIR; D64229; D64229. DR RefSeq; WP_010869401.1; NC_000908.2. DR ProteinModelPortal; P47508; -. DR STRING; 243273.MgenG_010200002609; -. DR PRIDE; P47508; -. DR EnsemblBacteria; AAC71488; AAC71488; MG_266. DR KEGG; mge:MG_266; -. DR PATRIC; 20010030; VBIMycGen98045_0307. DR eggNOG; ENOG4105C8T; Bacteria. DR eggNOG; COG0495; LUCA. DR KO; K01869; -. DR OMA; LGMFPYT; -. DR OrthoDB; EOG63Z74X; -. DR BioCyc; MGEN243273:GH2R-293-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:UniProtKB-HAMAP. 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; 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; 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 1 792 Leucine--tRNA ligase. FT /FTId=PRO_0000152045. FT MOTIF 39 50 "HIGH" region. FT MOTIF 569 573 "KMSKS" region. FT BINDING 572 572 ATP. {ECO:0000255|HAMAP-Rule:MF_00049}. FT CONFLICT 86 86 Q -> R (in Ref. 2; AAD10600). FT {ECO:0000305}. FT CONFLICT 225 225 W -> V (in Ref. 2; AAD12449). FT {ECO:0000305}. SQ SEQUENCE 792 AA; 91474 MW; D2146C8681E10DA5 CRC64; MYNHNLIEEK WLKKWKNKDV NRFESDSNKK KYYVLDMFPY PSAAGLHLGH VRAYTITDVI SRYYKAKGFN VIHPIGFDAF GLPAEQYAIN SNQNPGSWTD QNINNFINQL TSFGFDYDYH LSLKTTDPRY YKYTQWIFSE LFKANLAELV DIDVNWCEQL GTVLANEEVL IDSNGNAVSE RGSFSVEKRK MKQWVLKITT FADALLEGLD TLDWPEPIKE MQRNWIGKSK GVTINFQLKD HKEAIAIFTT KPQTIFGVSF LAVSTNHWLA KKIAETNKKV ASFLKKQLQK TTTLKQKATL YDGIDLLTNA IHPLTNELIP VYVANYVIEG YGTDAIMGVG AHNENDNFFA RKQKLKIINV IDKKERLQNS FAYNGLTTKE AQVAITNELI SQNKAKLTTV YKLRDWIFSR QRYWGEPFPI IFDENNTPHL VEQLPVELPL LENYKPDGSG NSPLMRNQAW VNIVKDNIHY QRETNTMPQW AGSCWYYLGY LMLIKNPNFW PIDSKEAKKL FDQYLPVDLY VGGAEHAVLH LLYARFWHKF LFDKKLVSTK EPFQKLINQG MVLGPDGKKM SKSKGNTINP TPLVDSHGAD ALRLYLMFMG PISASLTWND EGLNGMRRWL DRVYNFFFNH AVVTDQVSQE TIFAYNLFLK NSYCHLDKHE LNLVISEMMI FLNFLYKTKK ISLNYAKGFL TVLSFFAPFL AEELNEKCGL EPFVVKQAIS LVDYQLFETA KTKVILSING KFKAAKEFTK GSLEIDVLES FKQDKEINDI LNQPIERVVY VQDRIINVLL KK // ID SYM_MYCGE Reviewed; 512 AA. AC P47267; Q49339; Q49473; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 110. 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=MG021; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 440-508. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). 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: Monomer. {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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71237.1; -; Genomic_DNA. DR EMBL; U02229; AAA03382.2; -; Genomic_DNA. DR EMBL; X61513; CAA43727.1; -; Genomic_DNA. DR PIR; C64202; C64202. DR RefSeq; WP_009885919.1; NZ_AAGX01000010.1. DR ProteinModelPortal; P47267; -. DR STRING; 243273.MgenG_010200002776; -. DR EnsemblBacteria; AAC71237; AAC71237; MG_021. DR KEGG; mge:MG_021; -. DR PATRIC; 20009418; VBIMycGen98045_0019. DR eggNOG; ENOG4105CKH; Bacteria. DR eggNOG; COG0143; LUCA. DR KO; K01874; -. DR OMA; YIYKGSH; -. DR OrthoDB; EOG6CVV9B; -. DR BioCyc; MGEN243273:GH2R-21-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:UniProtKB-EC. DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1. DR InterPro; IPR014758; Met-tRNA_synth. DR InterPro; IPR023457; Met-tRNA_synth_2. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR Pfam; PF09334; tRNA-synt_1g; 2. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; SSF47323; 1. DR TIGRFAMs; TIGR00398; metG; 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 1 512 Methionine--tRNA ligase. FT /FTId=PRO_0000139228. FT MOTIF 11 21 "HIGH" region. FT MOTIF 301 305 "KMSKS" region. FT METAL 126 126 Zinc. {ECO:0000250}. FT METAL 129 129 Zinc. {ECO:0000250}. FT METAL 143 143 Zinc. {ECO:0000250}. FT METAL 147 147 Zinc. {ECO:0000250}. FT BINDING 304 304 ATP. {ECO:0000250}. FT CONFLICT 506 508 VLF -> FYL (in Ref. 3). {ECO:0000305}. SQ SEQUENCE 512 AA; 60007 MW; CA05EC9B4356F432 CRC64; MKRCYITTPI YYASGKPHIG HAFTTILADV IKRFKIQNGY EAFLLVGSDE HGNKIESKAK SLNLDPKTFV DINAQAFKLM WKTLNISFDH FIRTTDEIHK QQVQKTFQDL YDKKLIYQSE WKGAYCVECE QNYFTFNKQT MLCEIGHNLS LVQEPCWFIS FSSTKNWIET TIGKNQLNII PKSRASELKN NFINNGLNDL ALTRKNVTWG IKVPFDPNQT IYVWFDALFS YITNLGFRNG DPNFIKWWNN DNKEREVIHL ISREITRFHC IYWPIFLHLL DIKLPTQFLS HGWIVDGEGR KMSKSLNNVI SPEQLIDQFG VDGTRYCLLK EMRLDKDNRC SVSILKEIYN ADLANSFGNH VSRTFGMIKK YLNGKLEYQI ITDNALQKIM ILIDESIVQF DHYFNSYEFY RAINLLLKIV FELSKLIDDF KPWELFKNQE FSLLKQLLFT CVRCVQVCYV LLTPILVNTA SKVFHLFNFA DDACRKDQLR DATLLKKIII SNSMEVLFKR VD // ID SYS_MYCGE Reviewed; 417 AA. AC P47251; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 103. 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}; OrderedLocusNames=MG005; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8083173; RA Bailey C.C., Bott K.F.; RT "An unusual gene containing a dnaJ N-terminal box flanks the putative RT origin of replication of Mycoplasma genitalium."; RL J. Bacteriol. 176:5814-5819(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-112. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71221.1; -; Genomic_DNA. DR EMBL; U09251; AAA57073.1; -; Genomic_DNA. DR EMBL; U02210; AAD12502.1; -; Genomic_DNA. DR PIR; E64200; E64200. DR RefSeq; WP_010869286.1; NC_000908.2. DR ProteinModelPortal; P47251; -. DR STRING; 243273.MgenG_010200000020; -. DR EnsemblBacteria; AAC71221; AAC71221; MG_005. DR KEGG; mge:MG_005; -. DR PATRIC; 20009386; VBIMycGen98045_0005. DR eggNOG; ENOG4105CGR; Bacteria. DR eggNOG; COG0172; LUCA. DR KO; K01875; -. DR OMA; NTVRESI; -. DR OrthoDB; EOG61KBH9; -. DR BioCyc; MGEN243273:GH2R-5-MONOMER; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000000807; 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 1 417 Serine--tRNA ligase. FT /FTId=PRO_0000122079. FT NP_BIND 256 258 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}. FT NP_BIND 343 346 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}. FT REGION 225 227 Serine binding. {ECO:0000255|HAMAP- FT Rule:MF_00176}. FT BINDING 279 279 Serine. {ECO:0000255|HAMAP- FT Rule:MF_00176}. FT BINDING 379 379 Serine. {ECO:0000255|HAMAP- FT Rule:MF_00176}. SQ SEQUENCE 417 AA; 47987 MW; 5E43280A5915DDD0 CRC64; MLDPNKLRNN YDFFKKKLLE RNVNEQLLNQ FIQTDKLMRK NLQQLELANQ KQSLLAKQVA KQKDNKKLLA ESKELKQKIE NLNNAYKDSQ NISQDLLLNF PNIAHESVPV GKNESANLEL LKEGRKPVFD FKPLPHRELC EKLNLVAFDK ATKISGTRFV AYTDKAAKLL RAITNLMIDL NKSKYQEWNL PVVINELSLR STGQLPKFKD DVFKLENTRY YLSPTLEVQL INLHANEIFN EEDLPKYYTA TGINFRQEAG SAGKQTKGTI RLHQFQKTEL VKFCKPENAI NELEAMVRDA EQILKALKLP FRRLLLCTGD MGFSAEKTYD LEVWMAASNE YREVSSCSSC GDFQARRAMI RYKDINNGKN SYVATLNGTA LSIDRIFAAI LENFQTKDGK ILIPQALKKY LDFDTIK // ID SYW_MYCGE Reviewed; 347 AA. AC P47372; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 98. 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=MG126; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71344.1; -; Genomic_DNA. DR PIR; I64213; I64213. DR RefSeq; WP_009885680.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47372; -. DR SMR; P47372; 1-345. DR STRING; 243273.MgenG_010200000895; -. DR EnsemblBacteria; AAC71344; AAC71344; MG_126. DR KEGG; mge:MG_126; -. DR PATRIC; 20009656; VBIMycGen98045_0137. DR eggNOG; ENOG4105C31; Bacteria. DR eggNOG; COG0180; LUCA. DR KO; K01867; -. DR OMA; ATTDSFN; -. DR OrthoDB; EOG686NJQ; -. DR BioCyc; MGEN243273:GH2R-130-MONOMER; -. DR Proteomes; UP000000807; 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; 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. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 347 Tryptophan--tRNA ligase. FT /FTId=PRO_0000136646. FT MOTIF 11 19 "HIGH" region. FT MOTIF 200 204 "KMSKS" region. FT BINDING 203 203 ATP. {ECO:0000250}. SQ SEQUENCE 347 AA; 39328 MW; 82D1C572A523132B CRC64; MIKRAITGIQ ASGRQHLGNF LGVMQGLKQL QSQYQLFLFV ADLHAITVDF EPTMLKDNNL QLVKTLLALG LDYGKVNLFL QSDLMEHTML GYLMLTQSNL GELQRMTQFK TKKLAQKRNS NNTITIPTGL LTYPVLMAAD ILLYQPDIVP VGNDQKQHLE LTNDLAKRVA KKFKLKLKLP VFIENKDTNR IMDLSNPLKK MSKSNPDQNG VIYLDDSKET IIKKVRKATT DSFNKIRFAK KTQPGVTNLL VILTALLKEE VNHNLSKKIG SDLVKYYQNK SYLDLKNDLS SAVINVIESL KFKKAQITDE MVLKVLNDGK NQAKKVADET LKMFYKAFGL TSNQLFD // ID SYY_MYCGE Reviewed; 396 AA. AC P47693; Q49355; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 2. DT 13-APR-2016, entry version 110. DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02006}; DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006}; DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02006}; DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02006}; GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02006}; OrderedLocusNames=MG455; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-191. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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_02006}. CC -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP + CC diphosphate + L-tyrosyl-tRNA(Tyr). {ECO:0000255|HAMAP- CC Rule:MF_02006}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02006}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_02006}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA03403.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAC72475.1; 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; L43967; AAC72475.1; ALT_INIT; Genomic_DNA. DR EMBL; U02247; AAA03403.1; ALT_INIT; Genomic_DNA. DR PIR; C64250; C64250. DR RefSeq; WP_010869488.1; NC_000908.2. DR ProteinModelPortal; P47693; -. DR STRING; 243273.MgenG_010200000160; -. DR EnsemblBacteria; AAC72475; AAC72475; MG_455. DR KEGG; mge:MG_455; -. DR PATRIC; 20010500; VBIMycGen98045_0523. DR eggNOG; ENOG4105DA0; Bacteria. DR eggNOG; COG0162; LUCA. DR KO; K01866; -. DR OMA; AINQETD; -. DR OrthoDB; EOG6B09VR; -. DR BioCyc; MGEN243273:GH2R-508-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-HAMAP. 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_02006; Tyr_tRNA_synth_type1; 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; IPR002942; S4_RNA-bd. DR InterPro; IPR002307; Tyr-tRNA-ligase. DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type. DR InterPro; IPR024107; Tyr-tRNA-ligase_bac_1. 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; PS00178; AA_TRNA_LIGASE_I; 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 1 396 Tyrosine--tRNA ligase. FT /FTId=PRO_0000055657. FT DOMAIN 331 394 S4 RNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT MOTIF 41 50 "HIGH" region. FT MOTIF 225 229 "KMSKS" region. FT BINDING 36 36 Tyrosine. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT BINDING 165 165 Tyrosine. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT BINDING 169 169 Tyrosine. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT BINDING 228 228 ATP. {ECO:0000255|HAMAP-Rule:MF_02006}. FT CONFLICT 191 191 Q -> L (in Ref. 2; AAA03403). FT {ECO:0000305}. SQ SEQUENCE 396 AA; 45563 MW; 6638CC28DD57C16A CRC64; MLNNILQFLK ERELYSQANF ETELDNHLKE KKNNFYVGFD PTANSLHIGN YVLIHIAKLL KDMGHTPHIV LGSATALIGD PTGRIELRKI LEEKEIVKNT KTIKKQIKQF LGDVIIHENK VWLEKLNYIE VIRELGAFFS VNKMLSTDAF SARWEKGLTL MELNYMILQA YDFYYLHKNH NVTLQIGGSD QWANILAGAN LIKRKNNASV FGLTANLLVK ANGEKMGKTS SGALWLDENK TSVFDFYQYW INLDDQSLKK TFLMLTMLDK KVIDELCNLK GPKIKQTKQM LAFLITELIH GTKKAKEAQQ RSELIFSNQP DLDIKLVKTS TNLIDYLVET KFIKSKSEAR RLISQKGLTI NNKHVLDLNQ IIEWKEELQI IRKGKKSFLT IKTVNS // ID SYR_MYCGE Reviewed; 537 AA. AC P47618; Q49291; Q49444; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-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=MG378; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-255 AND 350-455. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71605.1; -; Genomic_DNA. DR EMBL; U02168; AAD12450.1; -; Genomic_DNA. DR EMBL; U01740; AAD10550.1; -; Genomic_DNA. DR PIR; H64241; H64241. DR RefSeq; WP_009885941.1; NZ_AAGX01000012.1. DR ProteinModelPortal; P47618; -. DR STRING; 243273.MgenG_010200002941; -. DR EnsemblBacteria; AAC71605; AAC71605; MG_378. DR KEGG; mge:MG_378; -. DR PATRIC; 20010338; VBIMycGen98045_0443. DR eggNOG; ENOG4107RUW; Bacteria. DR eggNOG; COG0018; LUCA. DR KO; K01887; -. DR OMA; QDLIYHL; -. DR OrthoDB; EOG6JB13C; -. DR BioCyc; MGEN243273:GH2R-433-MONOMER; -. DR Proteomes; UP000000807; 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; 3.40.50.620; -; 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; 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; PF05746; DALR_1; 1. DR Pfam; PF00750; tRNA-synt_1d; 1. DR PRINTS; PR01038; TRNASYNTHARG. DR SMART; SM00836; DALR_1; 1. DR SUPFAM; SSF47323; SSF47323; 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 1 537 Arginine--tRNA ligase. FT /FTId=PRO_0000151576. FT MOTIF 113 123 "HIGH" region. FT CONFLICT 153 154 YG -> MW (in Ref. 2). {ECO:0000305}. FT CONFLICT 350 355 FALQLV -> MHYNWI (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 537 AA; 62406 MW; D8080D69EDA33817 CRC64; MFFIINDLKE CISALKLKFD DQKELVKLVK NNSFNGFSST IIFQLKSENH KKIADSIVEW FLKNKKDNYQ NVFIANNNFI NFQISYQKYL EYLIKTPCFT KKNIKILIES VSANPTGRIH LGHVRIAFFG DVLNNLAKLL GYTTVCEYWV NDYGQQARVF SFSVYQSLQL KKNIAIQQHP DGYSGIVIDK IASEIENFPV DNLNFEEFCK TSFLDHFLVN CTQKVLSLIK SDLNKIHVFI DSWKFESEIV KKTNFNDLLE QLKPNSYFYQ DNALWLKTTL YGDDKDRVLI RSDKRASYFG TDVAYHLEKL QRGFDILFNV WGTDHEGHIK RMYCAFDALK NTTKTSLKIF ALQLVTLYKN KELVRLSKRA GNVITIETML SMISEDAARW FMLSQNNGTI IKIDLDIANL QNSANPVYYV QYAFARMNSI LRIANSDQLK EITDCSLLIN EKEISLLNQL VYYPFMLQKA METGELHLLT NFLYETASLF HSWYKVCKIN DDKNSLLSAQ RLALLRSLQF IVKQILDVLK ISTPQQM // ID SYV_MYCGE Reviewed; 837 AA. AC P47576; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 104. 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}; OrderedLocusNames=MG334; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 801-837. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71557.1; -; Genomic_DNA. DR EMBL; U02249; AAD12537.1; -; Genomic_DNA. DR PIR; I64236; I64236. DR RefSeq; WP_010869437.1; NC_000908.2. DR ProteinModelPortal; P47576; -. DR STRING; 243273.MgenG_010200003096; -. DR EnsemblBacteria; AAC71557; AAC71557; MG_334. DR KEGG; mge:MG_334; -. DR PATRIC; 20010224; VBIMycGen98045_0389. DR eggNOG; ENOG4105CA4; Bacteria. DR eggNOG; COG0525; LUCA. DR KO; K01873; -. DR OMA; ICEQLRV; -. DR OrthoDB; EOG644ZM1; -. DR BioCyc; MGEN243273:GH2R-382-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:UniProtKB-HAMAP. DR GO; GO:0006438; P:valyl-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_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; 1. 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 1 837 Valine--tRNA ligase. FT /FTId=PRO_0000106230. FT COILED 767 837 {ECO:0000255|HAMAP-Rule:MF_02004}. FT MOTIF 46 56 "HIGH" region. FT MOTIF 514 518 "KMSKS" region. FT BINDING 517 517 ATP. {ECO:0000255|HAMAP-Rule:MF_02004}. SQ SEQUENCE 837 AA; 97464 MW; 7F2FD1FE95D3D8C5 CRC64; MKDKFSFQKN YDFNLVSDGL YEIWNNAGFF KPKDKNNSFT AILPPPNLTG TLHIGHAFEV SITDQIMRFK KMQGFSINWI PGFDHAGIAT QTKYEKIALK ENQKYFDADD DKKSEMIMNW ALNQSEIIKN QLKSLGVCLN WSETKFTLSE QANKIVNNCF KNLYENGFIY QAYTLVNWDT KLNTAISNIE VINKPVNQHL HYVVYKLAND SKQELIVATT RPETIFADVC LLVNPKDKRY TNFWNKLVVN PLTGKQIPVV TDSYVDIKFG TGILKCTPAH DFNDYEINTK YKFDFLSCID SNGILNQNAS KFQGLSVLQA RNKIVKWLEK NKLLVKSIPL TSNVGFSERS GTVVEPMLSK QWFVDLPKLK DHLYLKKYPD FIPKRFNKQV SNWLNKLKPW CISRQLIWGH KIPVWFENNT GEIVVGEKPS KNLQNYTRSK DVLDTWFSSS LWPLICLNWE QDDSFHETEL LVTGYDILFF WVLRMLFNSF FETKKLPFKT VLIHGLVRDE QNRKMSKSLN NGIDPVDLIR NYGADAVRLF LCSNHTPGDD LIFSEQKIKS AWNFLNKLWN VTKFVIQLEN DQEISYDLDK LSLSETWILA KLDKVIQKIT KLLDKFQLAL ANQILVKFVW DDFCNTFIEA IKKEPNQLKP QLFYTAKSVL SNIAILLSIT VPFLSERIYQ QFNNKSVMQA TWPLATKIKI PKLFDLVLAA INDLRNYRKQ YMLNSQQKLV VILSGKNAVD VKQYFNFSWI ELKIETNKKV SFKYQIVDDT TQRLKSLQKQ QAFFESEVKR SQAIVKNKSF LEKAPKEKVK SEFLKLEEYQ KKLTETNQLI AKLTKAH // ID T1SX_MYCGE Reviewed; 383 AA. AC Q49434; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 84. DE RecName: Full=Putative type-1 restriction enzyme specificity protein MG438; DE AltName: Full=S.MgeORF438P; DE AltName: Full=Type I restriction enzyme specificity protein MG438; DE Short=S protein; GN OrderedLocusNames=MG438; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. Subunit S CC dictates DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase 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; L43967; AAC72457.1; -; Genomic_DNA. DR PIR; D64248; D64248. DR RefSeq; WP_009885596.1; NZ_AAGX01000001.1. DR PDB; 1YDX; X-ray; 2.30 A; A=1-383. DR PDBsum; 1YDX; -. DR ProteinModelPortal; Q49434; -. DR SMR; Q49434; 1-374. DR STRING; 243273.MgenG_010200000275; -. DR REBASE; 3674; S.MgeORF438P. DR EnsemblBacteria; AAC72457; AAC72457; MG_438. DR KEGG; mge:MG_438; -. DR PATRIC; 20010460; VBIMycGen98045_0503. DR eggNOG; ENOG41060B8; Bacteria. DR eggNOG; COG0732; LUCA. DR OMA; RDEYAHK; -. DR OrthoDB; EOG654P1V; -. DR BioCyc; MGEN243273:GH2R-491-MONOMER; -. DR EvolutionaryTrace; Q49434; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-binding; Reference proteome; KW Restriction system. FT CHAIN 1 383 Putative type-1 restriction enzyme FT specificity protein MG438. FT /FTId=PRO_0000198042. FT STRAND 7 10 {ECO:0000244|PDB:1YDX}. FT STRAND 14 17 {ECO:0000244|PDB:1YDX}. FT HELIX 18 21 {ECO:0000244|PDB:1YDX}. FT STRAND 22 26 {ECO:0000244|PDB:1YDX}. FT HELIX 32 34 {ECO:0000244|PDB:1YDX}. FT STRAND 40 49 {ECO:0000244|PDB:1YDX}. FT STRAND 53 55 {ECO:0000244|PDB:1YDX}. FT STRAND 64 67 {ECO:0000244|PDB:1YDX}. FT STRAND 69 71 {ECO:0000244|PDB:1YDX}. FT STRAND 75 77 {ECO:0000244|PDB:1YDX}. FT STRAND 82 84 {ECO:0000244|PDB:1YDX}. FT STRAND 88 94 {ECO:0000244|PDB:1YDX}. FT TURN 96 98 {ECO:0000244|PDB:1YDX}. FT HELIX 101 109 {ECO:0000244|PDB:1YDX}. FT HELIX 112 116 {ECO:0000244|PDB:1YDX}. FT STRAND 122 124 {ECO:0000244|PDB:1YDX}. FT HELIX 129 134 {ECO:0000244|PDB:1YDX}. FT STRAND 136 139 {ECO:0000244|PDB:1YDX}. FT HELIX 143 182 {ECO:0000244|PDB:1YDX}. FT HELIX 186 191 {ECO:0000244|PDB:1YDX}. FT HELIX 196 200 {ECO:0000244|PDB:1YDX}. FT STRAND 202 205 {ECO:0000244|PDB:1YDX}. FT HELIX 206 208 {ECO:0000244|PDB:1YDX}. FT STRAND 210 214 {ECO:0000244|PDB:1YDX}. FT HELIX 220 222 {ECO:0000244|PDB:1YDX}. FT STRAND 224 226 {ECO:0000244|PDB:1YDX}. FT STRAND 228 237 {ECO:0000244|PDB:1YDX}. FT STRAND 239 244 {ECO:0000244|PDB:1YDX}. FT STRAND 249 255 {ECO:0000244|PDB:1YDX}. FT TURN 259 262 {ECO:0000244|PDB:1YDX}. FT STRAND 264 269 {ECO:0000244|PDB:1YDX}. FT STRAND 271 273 {ECO:0000244|PDB:1YDX}. FT STRAND 277 284 {ECO:0000244|PDB:1YDX}. FT HELIX 289 310 {ECO:0000244|PDB:1YDX}. FT HELIX 317 321 {ECO:0000244|PDB:1YDX}. FT STRAND 324 327 {ECO:0000244|PDB:1YDX}. FT HELIX 331 369 {ECO:0000244|PDB:1YDX}. SQ SEQUENCE 383 AA; 44111 MW; 38A8341227AEEC65 CRC64; MTPKLKLNNN INWTKRTIDS LFDLKKGEML EKELITPEGK YEYFNGGVKN SGRTDKFNTF KNTISVIVGG SCGYVRLADK NFFCGQSNCT LNLLDPLELD LKFAYYALKS QQERIEALAF GTTIQNIRIS DLKELEIPFT SNKNEQHAIA NTLSVFDERL ENLASLIEIN RKLRDEYAHK LFSLDEAFLS HWKLEALQSQ MHEITLGEIF NFKSGKYLKS EERLEEGKFP YYGAGIDNTG FVAEPNTEKD TISIISNGYS LGNIRYHEIP WFNGTGSIAL EPMNNEIYVP FFYCALKYLQ KDIKERMKSD DSPFLSLKLA GEIKVPYVKS FQLQRKAGKI VFLLDQKLDQ YKKELSSLTV IRDTLLKKLF PDMTERTKSI KDY // ID TKT_MYCGE Reviewed; 648 AA. AC P47312; Q49280; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Transketolase; DE Short=TK; DE EC=2.2.1.1; GN Name=tkt; Synonyms=tktA; OrderedLocusNames=MG066; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from CC a ketose donor to an aldose acceptor, via a covalent intermediate CC with the cofactor thiamine pyrophosphate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other CC divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+). CC {ECO:0000250}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the transketolase 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; L43967; AAC71284.1; -; Genomic_DNA. DR EMBL; U02154; AAD12435.1; -; Genomic_DNA. DR PIR; C64207; C64207. DR RefSeq; WP_010869316.1; NC_000908.2. DR ProteinModelPortal; P47312; -. DR EnsemblBacteria; AAC71284; AAC71284; MG_066. DR KEGG; mge:MG_066; -. DR PATRIC; 20009518; VBIMycGen98045_0068. DR KO; K00615; -. DR OMA; ESKDAKF; -. DR OrthoDB; EOG6N3CRG; -. DR BioCyc; MGEN243273:GH2R-69-MONOMER; -. DR Proteomes; UP000000807; 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; IPR005478; Transketolase_bac-like. DR InterPro; IPR020826; Transketolase_BS. DR InterPro; IPR033247; Transketolase_fam. DR InterPro; IPR005474; Transketolase_N. DR PANTHER; PTHR11624; PTHR11624; 2. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF00456; Transketolase_N; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR SUPFAM; SSF52922; SSF52922; 1. DR TIGRFAMs; TIGR00232; tktlase_bact; 1. DR PROSITE; PS00802; TRANSKETOLASE_2; 1. PE 3: Inferred from homology; KW Calcium; Complete proteome; Magnesium; Metal-binding; KW Reference proteome; Thiamine pyrophosphate; Transferase. FT CHAIN 1 648 Transketolase. FT /FTId=PRO_0000191859. FT NP_BIND 109 111 Thiamine pyrophosphate. {ECO:0000250}. FT ACT_SITE 397 397 Proton donor. {ECO:0000250}. FT METAL 150 150 Magnesium. {ECO:0000250}. FT METAL 180 180 Magnesium. {ECO:0000250}. FT METAL 182 182 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 22 22 Substrate. {ECO:0000250}. FT BINDING 62 62 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 151 151 Thiamine pyrophosphate; via amide FT nitrogen. {ECO:0000250}. FT BINDING 180 180 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 252 252 Substrate. {ECO:0000250}. FT BINDING 252 252 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 345 345 Substrate. {ECO:0000250}. FT BINDING 372 372 Substrate. {ECO:0000250}. FT BINDING 423 423 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 447 447 Substrate. {ECO:0000250}. FT BINDING 455 455 Substrate. {ECO:0000250}. FT BINDING 506 506 Substrate. {ECO:0000250}. FT SITE 22 22 Important for catalytic activity. FT {ECO:0000250}. FT SITE 252 252 Important for catalytic activity. FT {ECO:0000250}. FT CONFLICT 24 24 G -> C (in Ref. 2; AAD12435). FT {ECO:0000305}. SQ SEQUENCE 648 AA; 73785 MW; 0252E8DDD2BFB453 CRC64; MKYLYATQHL TLNAIKHAKG GHVGMAIGAS PILFSLFTKH FHFDPDQPKW INRDRFVLSA GHGSMALYSI FHFAGLISKQ EILQHKHGQI NTSSHPEYAP NNFIDASTGP LGQGFGMAVG MVLAQKLLAN EFKELSDKLF DHYTYVVVGD GDLQEGVSYE VSQIAGLYKL NKLIVLHDSN RVQMDSEVKK VANENLKVRF ENVGWNYIHT DDQLENIDQA IIKAKQSDKP TFIEVRTTIA KNTHLEDQYG GHWFIPNEVD FQLFEKRTNT NFNFFNYPDS IYHWFKQTVI ERQKQIKEDY NNLLISLKDK PLFKKFTNWI DSDFQALYLN QLDEKKVAKK DSATRNYLKD FLNQINNPNS NLYCLNADVS RSCFIKIGDD NLHENPCSRN IQIGIREFAM ATIMNGMALH GGIKVMGGTF LAFADYSKPA IRLGALMNLP VFYVYTHDSY QVGGDGPTHQ PYDQLPMLRA IENVCVFRPC DEKETCAGFN YGLLSQDQTT VLVLTRQPLK SIDNTDSLKT LKGGYILLDR KQPDLIIAAS GSEVQLAIEF EKVLTKQNVK VRILSVPNIT LLLKQDEKYL KSLFDANSSL ITIEASSSYE WFCFKKYVKN HAHLGAFSFG ESDDGDKVYQ QKGFNLERLM KIFTSLRN // ID THIO_MYCGE Reviewed; 102 AA. AC P47370; Q49453; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Thioredoxin; DE Short=Trx; GN Name=trxA; Synonyms=trx; OrderedLocusNames=MG124; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Participates in various redox reactions through the CC reversible oxidation of its active center dithiol to a disulfide CC and catalyzes dithiol-disulfide exchange reactions. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00691}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD12321.1; 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; L43967; AAC71342.1; -; Genomic_DNA. DR EMBL; U01796; AAD12321.1; ALT_INIT; Genomic_DNA. DR PIR; G64213; G64213. DR RefSeq; WP_010869343.1; NC_000908.2. DR ProteinModelPortal; P47370; -. DR EnsemblBacteria; AAC71342; AAC71342; MG_124. DR KEGG; mge:MG_124; -. DR PATRIC; 20009652; VBIMycGen98045_0135. DR OMA; ESYQQFQ; -. DR OrthoDB; EOG6QG8RK; -. DR BioCyc; MGEN243273:GH2R-128-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR005746; Thioredoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR10438; PTHR10438; 1. DR Pfam; PF00085; Thioredoxin; 1. DR PIRSF; PIRSF000077; Thioredoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR01068; thioredoxin; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome; Disulfide bond; Electron transport; KW Redox-active center; Reference proteome; Transport. FT CHAIN 1 102 Thioredoxin. FT /FTId=PRO_0000120113. FT DOMAIN 2 102 Thioredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. FT DISULFID 30 33 Redox-active. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. SQ SEQUENCE 102 AA; 11498 MW; FC08F02C4170EA2D CRC64; MVTEIRSLKQ LEEIFSAKKN VIVDFWAAWC GPCKLTSPEF QKAADEFSDA QFVKVNVDDH TDIAAAYNIT SLPTIVVFEN GVEKKRAIGF MPKTKIIDLF NN // ID TILS_MYCGE Reviewed; 290 AA. AC P47330; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 95. 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}; OrderedLocusNames=MG084; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 266-290. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71302.1; -; Genomic_DNA. DR EMBL; U01783; AAD10603.1; -; Genomic_DNA. DR PIR; C64209; C64209. DR RefSeq; WP_010869324.1; NC_000908.2. DR ProteinModelPortal; P47330; -. DR EnsemblBacteria; AAC71302; AAC71302; MG_084. DR KEGG; mge:MG_084; -. DR PATRIC; 20009570; VBIMycGen98045_0094. DR KO; K04075; -. DR OMA; VAHINYN; -. DR OrthoDB; EOG6NKR0V; -. DR BioCyc; MGEN243273:GH2R-87-MONOMER; -. DR Proteomes; UP000000807; 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; 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; 2. DR Pfam; PF01171; ATP_bind_3; 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 1 290 tRNA(Ile)-lysidine synthase. FT /FTId=PRO_0000181727. FT NP_BIND 12 17 ATP. {ECO:0000255|HAMAP-Rule:MF_01161}. SQ SEQUENCE 290 AA; 34629 MW; B8C09B71FD8156A1 CRC64; MASEKQYIAG VSGGSDSMLM LKLYQKKIAC VVHVNYNTRS TSLRDQKLVE QYCQKLNIPL VVHTVDPDLV WKKNFQNQAR KIRFDQFKKT AKLYQTNKLL LAHHRDDFIE QAKMQLDAKK RAVYYGIKTR CELYGLKIYR PLMKYWKDEI IALCRQDHIP YEIDETNKLP IYKRNEVRLE IEKWSKIEKE QFYIAICAMN KTIAQKLFVL MKKAKKWLLQ PDVRELKRFS IIDQKQLIYS YLIYHKINVN GEKIDAILDF IQPSQQKQYR LQNDIFLMVK NQCLALLYKS // ID THII_MYCGE Reviewed; 385 AA. AC P47612; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 99. 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}; OrderedLocusNames=MG372; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71599.1; -; Genomic_DNA. DR PIR; B64241; B64241. DR RefSeq; WP_009885937.1; NZ_AAGX01000012.1. DR ProteinModelPortal; P47612; -. DR STRING; 243273.MgenG_010200002911; -. DR EnsemblBacteria; AAC71599; AAC71599; MG_372. DR KEGG; mge:MG_372; -. DR PATRIC; 20010326; VBIMycGen98045_0437. DR eggNOG; ENOG4105D8I; Bacteria. DR eggNOG; COG0301; LUCA. DR KO; K03151; -. DR OMA; PDEDCCT; -. DR OrthoDB; EOG6TBHGR; -. DR BioCyc; MGEN243273:GH2R-427-MONOMER; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; KW Reference proteome; RNA-binding; Thiamine biosynthesis; Transferase; KW tRNA-binding. FT CHAIN 1 385 Probable tRNA sulfurtransferase. FT /FTId=PRO_0000154849. FT DOMAIN 65 165 THUMP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT NP_BIND 183 184 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT NP_BIND 208 209 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 267 267 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 285 285 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 294 294 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. SQ SEQUENCE 385 AA; 44177 MW; E2A1A300077220CF CRC64; MELNSEDVLV ARYGELVLKG KNRSYFTKQL KINIKKAFKK LEINNSIVYE FDRIVVFDIK KEQRAILQEL FSFLPGISLF FFASQIVREE NKLLDLLFNL FKDFNSFKLE VKRRDKNFAE NSSNFKKYLA VKLFEKYQLK GVINNPEIIA NIEILKEHFL VFTERFKGKG GLPVYSSGKA LVLLSGGIDS PVAASLVMQR GFNIDFITFI NEPNKNQKTI EKITRLANLI SFNKTICSGK LLVFDFTAIQ KELIHISNES YRIVLMRRVF YKAASMFKYD CLVTGEVLGQ VASQTIENLK VIQSATPDTF IVRPLIGFSK DKIIELAKFF NTFDISIEQH LDTCSEFSPK NPTTKAKLIN VEKLESELIF LNDLIEKGVS ELSND // ID TIG_MYCGE Reviewed; 444 AA. AC P47480; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=Trigger factor; DE Short=TF; DE EC=5.2.1.8; DE AltName: Full=PPIase; GN Name=tig; OrderedLocusNames=MG238; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-216. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [3] RP STRUCTURE BY NMR OF 166-250. RX PubMed=12054805; DOI=10.1016/S0022-2836(02)00112-2; RA Vogtherr M., Jacobs D.M., Parac T.N., Maurer M., Pahl A., Saxena K., RA Rueterjans H., Griesinger C., Fiebig K.M.; RT "NMR solution structure and dynamics of the peptidyl-prolyl cis-trans RT isomerase domain of the trigger factor from Mycoplasma genitalium RT compared to FK506-binding protein."; RL J. Mol. Biol. 318:1097-1115(2002). 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 -!- 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; L43967; AAC71459.1; -; Genomic_DNA. DR EMBL; U01772; AAD10591.1; -; Genomic_DNA. DR PIR; C64226; C64226. DR RefSeq; WP_009885775.1; NZ_AAGX01000005.1. DR PDB; 1HXV; NMR; -; A=150-250. DR PDBsum; 1HXV; -. DR ProteinModelPortal; P47480; -. DR SMR; P47480; 166-250. DR STRING; 243273.MgenG_010200001617; -. DR EnsemblBacteria; AAC71459; AAC71459; MG_238. DR KEGG; mge:MG_238; -. DR PATRIC; 20009958; VBIMycGen98045_0275. DR eggNOG; ENOG4108007; Bacteria. DR eggNOG; COG0544; LUCA. DR KO; K03545; -. DR OMA; LVHEELM; -. DR OrthoDB; EOG63VBX3; -. DR BioCyc; MGEN243273:GH2R-260-MONOMER; -. DR EvolutionaryTrace; P47480; -. DR Proteomes; UP000000807; 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; IPR001179; PPIase_FKBP_dom. 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; PF00254; FKBP_C; 1. 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. DR PROSITE; PS50059; FKBP_PPIASE; 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 1 444 Trigger factor. FT /FTId=PRO_0000179382. FT DOMAIN 170 255 PPIase FKBP-type. FT STRAND 169 181 {ECO:0000244|PDB:1HXV}. FT STRAND 192 198 {ECO:0000244|PDB:1HXV}. FT HELIX 207 212 {ECO:0000244|PDB:1HXV}. FT STRAND 216 222 {ECO:0000244|PDB:1HXV}. FT STRAND 230 233 {ECO:0000244|PDB:1HXV}. FT HELIX 234 236 {ECO:0000244|PDB:1HXV}. FT STRAND 241 246 {ECO:0000244|PDB:1HXV}. SQ SEQUENCE 444 AA; 50931 MW; 99704A2EA4E23F47 CRC64; MKLYKVLNSK TTDKSLCLEV EIDPNYWQAT QKKLVGEMAK SIKIKGFRPG KIPPNLASQS INKAELMQKS AQNVMNSIYE SVQQEEIVAS NDNVIDDYPT IDFKTITEQN CVLLFYFDLI PNFQLPDYKK IKDLTPLTKL TEAEFNNEIE KLAKTKSTMV DVSDKKLANG DIAIIDFTGI VDNKKLASAS AQNYELTIGS NSFIKGFETG LIAMKVNQKK TLALTFPSDY HVKELQSKPV TFEVVLKAIK KLEFTPMDET NFKSFLPEQF QSFTSLKAFK SYFHKLMENK KQETILQENN QKIRQFLLTN TKLPFLPEAL IKLEANRLLK LQQSQAEQYK IPFEKLLSAS NITLTELQDR NIKEAKENVT FALVMKKIAD IEKIKVDNNK IKAEIENVIA VEYPFASDEM KKQLFFNMEQ QKEFVESIII NRLTTTKIVS YSTH // ID TRMD_MYCGE Reviewed; 231 AA. AC P47683; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 98. 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=MG445; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC72465.1; -; Genomic_DNA. DR PIR; B64249; B64249. DR RefSeq; WP_010869485.1; NC_000908.2. DR ProteinModelPortal; P47683; -. DR STRING; 243273.MgenG_010200000225; -. DR EnsemblBacteria; AAC72465; AAC72465; MG_445. DR KEGG; mge:MG_445; -. DR PATRIC; 20010478; VBIMycGen98045_0512. DR eggNOG; ENOG4105D6X; Bacteria. DR eggNOG; COG0336; LUCA. DR KO; K00554; -. DR OMA; NRYDLYL; -. DR OrthoDB; EOG6J48RZ; -. DR BioCyc; MGEN243273:GH2R-498-MONOMER; -. DR Proteomes; UP000000807; 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 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 1 231 tRNA (guanine-N(1)-)-methyltransferase. FT /FTId=PRO_0000060412. FT REGION 129 134 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 110 110 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000250}. SQ SEQUENCE 231 AA; 26478 MW; 71297CB5FF45C158 CRC64; MKITVLTLFE NTIWPYLNSS IMLQAQKANL VQFEVVNWRN FCNDKHKTVD DMAYGGGSGM VLKAEPIINC LNFYKAPNSH VVLLSPEGEQ FSQNCAKKLT KYEHLILLSG HYEGFDQRIY KYIDQIVSLG DFVLSGGELV ALSVIDATVR LIKGVINDQS LICESFNDNL LDFPVYTRPY DLKGDKVPEV LLSGDHQKIE SFRKEQQILK TAKYRPDLYK KYLENKNEKN K // ID TRML_MYCGE Reviewed; 166 AA. AC P47588; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=Putative tRNA (cytidine(34)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01885}; DE EC=2.1.1.207 {ECO:0000255|HAMAP-Rule:MF_01885}; DE AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01885}; GN OrderedLocusNames=MG346; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Could methylate the ribose at the nucleotide 34 wobble CC position in tRNA. {ECO:0000255|HAMAP-Rule:MF_01885}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytidine(34) in tRNA CC = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(34) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_01885}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 5- CC carboxymethylaminomethyluridine(34) in tRNA(Leu) = S-adenosyl-L- CC homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine(34) CC in tRNA(Leu). {ECO:0000255|HAMAP-Rule:MF_01885}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01885}. CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase TrmH family. CC TrmL subfamily. {ECO:0000255|HAMAP-Rule:MF_01885}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71571.1; -; Genomic_DNA. DR PIR; C64238; C64238. DR RefSeq; WP_009885804.1; NZ_AAGX01000006.1. DR ProteinModelPortal; P47588; -. DR STRING; 243273.MgenG_010200001858; -. DR EnsemblBacteria; AAC71571; AAC71571; MG_346. DR KEGG; mge:MG_346; -. DR PATRIC; 20010258; VBIMycGen98045_0406. DR eggNOG; ENOG4108UIQ; Bacteria. DR eggNOG; COG0219; LUCA. DR KO; K03216; -. DR OMA; INLANCV; -. DR OrthoDB; EOG6RG038; -. DR BioCyc; MGEN243273:GH2R-396-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_01885; tRNA_methyltr_TrmL; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR016914; tRNA_cyt/urid_MeTfrase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF00588; SpoU_methylase; 1. DR PIRSF; PIRSF029256; SpoU_TrmH_prd; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00185; tRNA_yibK_trmL; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 166 Putative tRNA (cytidine(34)-2'-O)- FT methyltransferase. FT /FTId=PRO_0000159835. FT BINDING 83 83 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01885}. FT BINDING 109 109 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01885}. FT BINDING 130 130 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01885}. FT BINDING 138 138 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01885}. SQ SEQUENCE 166 AA; 19314 MW; 185AEA122B7CF67D CRC64; MYKSVINIVL FCPEIPNNTG NIVRSCTAFK ANLHLIKPYG FFLNDKRMVR AGLNCWDKIQ LFEHKSWEHF LQATTENKTI WLLTKSGDKT PDQICMTNKL PNELYFVFGQ ETKGLPKTIM DNFKQNQIRI PIWNSVRSIN LANAVVCILY EYSKQNQYSN LDKQCA // ID TOP1_MYCGE Reviewed; 709 AA. AC P47368; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 117. 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}; OrderedLocusNames=MG122; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-481 AND 527-657. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71340.1; -; Genomic_DNA. DR EMBL; U02134; AAD12411.1; -; Genomic_DNA. DR EMBL; U02242; AAA03398.1; -; Genomic_DNA. DR PIR; E64213; E64213. DR RefSeq; WP_009885678.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47368; -. DR STRING; 243273.MgenG_010200000865; -. DR EnsemblBacteria; AAC71340; AAC71340; MG_122. DR KEGG; mge:MG_122; -. DR PATRIC; 20009648; VBIMycGen98045_0133. DR eggNOG; ENOG4105C73; Bacteria. DR eggNOG; COG0550; LUCA. DR eggNOG; COG0551; LUCA. DR KO; K03168; -. DR OMA; CSKFPKC; -. DR OrthoDB; EOG6S7XQ9; -. DR BioCyc; MGEN243273:GH2R-126-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. 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; IPR013498; Topo_IA_Znf. DR InterPro; IPR005733; TopoI_bac-type. DR InterPro; IPR028612; Topoisom_1_IA. DR InterPro; IPR006171; Toprim_domain. DR PANTHER; PTHR11390; PTHR11390; 2. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF01396; zf-C4_Topoisom; 2. 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 3: Inferred from homology; KW Complete proteome; DNA-binding; Isomerase; Magnesium; Metal-binding; KW Reference proteome; Repeat; Topoisomerase; Zinc; Zinc-finger. FT CHAIN 1 709 DNA topoisomerase 1. FT /FTId=PRO_0000145155. FT DOMAIN 3 127 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT ZN_FING 618 646 C4-type 1. FT ZN_FING 667 696 C4-type 2. FT REGION 176 181 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT ACT_SITE 334 334 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 9 9 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 95 95 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 95 95 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT METAL 97 97 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 34 34 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 153 153 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 157 157 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 336 336 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 529 529 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. SQ SEQUENCE 709 AA; 82545 MW; 1153189668672B5D CRC64; MIKNLVVIES PNKVKTLKQY LPSDEFEIVS TVGHIREMVY KNFGFDENTY TPIWEDWTKN KQKNPKQKHL LSKFEIIKSI KAKASDAQNI FLASDPDREG EAISWHVYDL LDQKDKAKCK RITFNEITKK AVVDALKQPR NIDLNWVESQ FARQILDRMI GFRLSRLLNS YLQAKSAGRV QSVALRFLEE REKEIAKFVP RFWWTVDVLL NKENNQKVVC ANKSIPLVLR EINPELSASL KLDFEAAENV SGIDFLNEAS ATRFANQLTG EYEVYFIDEP KIYYSSPNPV YTTASLQKDA INKLGWSSKK VTMVAQRLYE GISVNGKQTA LISYPRTDSI RISNQFQSEC EKYIEKEFGS HYLADKNKLK RHKKDEKIIQ DAHEGIHPTY ITITPNDLKN GVKRDEFLLY RLIWIRTVAS LMADAKTSRT IVRFINQKNK FYTSSKSLLF DGYQRLYEEI KPNTKDELYI DLSKLKIGDK FSFEKISVNE HKTNPPPRYT QASLIEELEK SNIGRPSTYN TMASVNLERG YANLVNRFFY ITELGEKVNN ELSKHFGNVI NKEFTKKMEK SLDEIAENKV NYQEFLKQFW TNFKSDVKLA ENSIQKVKKE KELVERDCPK CNQPLVYRYT KRGNEKFVGC SDFPKCKYSE FSNPKPKLTL ETLDELCPEC NNKLVKRRTK FNAKKTFIGC SNFPNCRFIK KDNAAEFKQ // ID TPIS_MYCGE Reviewed; 244 AA. AC P47670; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147}; DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147}; DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147}; DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147}; DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147}; GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; Synonyms=tim, tpi; GN OrderedLocusNames=MG431; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 155-244. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes CC stereospecifically the conversion of dihydroxyacetone phosphate CC (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP- CC Rule:MF_00147}. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00147}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00147}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC72452.1; -; Genomic_DNA. DR EMBL; U02109; AAD12380.1; -; Genomic_DNA. DR PIR; F64247; F64247. DR RefSeq; WP_009885602.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47670; -. DR STRING; 243273.MgenG_010200000305; -. DR EnsemblBacteria; AAC72452; AAC72452; MG_431. DR KEGG; mge:MG_431; -. DR PATRIC; 20010448; VBIMycGen98045_0497. DR eggNOG; ENOG4105CP7; Bacteria. DR eggNOG; COG0149; LUCA. DR KO; K01803; -. DR OMA; IEKNGTM; -. DR OrthoDB; EOG66QM23; -. DR BioCyc; MGEN243273:GH2R-485-MONOMER; -. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004807; F:triose-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 GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00147_B; TIM_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022896; TrioseP_Isoase_bac/euk. DR InterPro; IPR000652; Triosephosphate_isomerase. DR InterPro; IPR020861; Triosephosphate_isomerase_AS. DR PANTHER; PTHR21139; PTHR21139; 1. DR Pfam; PF00121; TIM; 1. DR SUPFAM; SSF51351; SSF51351; 1. DR TIGRFAMs; TIGR00419; tim; 1. DR PROSITE; PS00171; TIM_1; 1. DR PROSITE; PS51440; TIM_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; KW Pentose shunt; Reference proteome. FT CHAIN 1 244 Triosephosphate isomerase. FT /FTId=PRO_0000090247. FT REGION 9 11 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 93 93 Electrophile. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 160 160 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT BINDING 166 166 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00147}. FT BINDING 206 206 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00147}. SQ SEQUENCE 244 AA; 27344 MW; 2AE85F4EBEE36C4D CRC64; MRTRYLIGNW KTNKNLKDAV SFVEQFQQNK LNYNAKIGIA PVYVHLTEIK KIISDSLLLF AQDANFIESG SYTGTVSFTQ LQDIGVNNSI IGHSERRKYY NETSAVINQK LFACLKASMQ VVLCIGEALG QEISFLKTDL TNCLDTIDKS LIKNLVIAYE PLWAIGTGKT ATPEVANQTI KTIREYINDL YDENVANNIS ILYGGSVDHN NIQKLAIMEQ IDGFLVGKAS LEIKNFLEMA RVYA // ID TSAD_MYCGE Reviewed; 315 AA. AC P47292; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 103. 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=MG046; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71262.1; -; Genomic_DNA. DR PIR; A64205; A64205. DR RefSeq; WP_009885708.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47292; -. DR STRING; 243273.MgenG_010200001095; -. DR EnsemblBacteria; AAC71262; AAC71262; MG_046. DR KEGG; mge:MG_046; -. DR PATRIC; 20009470; VBIMycGen98045_0045. DR eggNOG; ENOG4105CPM; Bacteria. DR eggNOG; COG0533; LUCA. DR KO; K01409; -. DR OMA; YTKEPGL; -. DR OrthoDB; EOG6K402S; -. DR BioCyc; MGEN243273:GH2R-46-MONOMER; -. DR Proteomes; UP000000807; 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; IEA:InterPro. DR HAMAP; MF_01445; TsaD; 1. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR017861; KAE1/TsaD. DR InterPro; IPR017860; Peptidase_M22_CS. 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. DR PROSITE; PS01016; GLYCOPROTEASE; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Iron; Metal-binding; KW Reference proteome; Transferase; tRNA processing. FT CHAIN 1 315 tRNA N6-adenosine FT threonylcarbamoyltransferase. FT /FTId=PRO_0000096967. FT REGION 135 139 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT METAL 110 110 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT METAL 114 114 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT METAL 297 297 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT BINDING 168 168 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT BINDING 181 181 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01445}. FT BINDING 185 185 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT BINDING 273 273 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. SQ SEQUENCE 315 AA; 34708 MW; D186ECD176C4E574 CRC64; MEQPLCVLGI ETTCDDTGLS IVIDQKIKSN IVISSANLHV KTGGVVPEIA ARCHEQNLFK AIRDLNFEIR DLSHIAYACN PGLAGCLHVG ATFARSLSFL LDKPLLPINH LYAHIFSCLI DQDLNKLQLP ALGLVISGGH TAIYLVKSFY ELELIAETSD DAIGEVYDKI GRAMGFDYPA GSKIDSLFNK ELVKPHYFFK PSTKWTKFSY SGLKSQCLNK IKQISANKTR IDWSELASNF QATIIDHYID HVKNAIKKFA PKMLLVGGGV SANSYLSNRI STLNLPFLIA DSKYTSDNGA MIGFYASLLI NGDKN // ID TRMB_MYCGE Reviewed; 210 AA. AC P47589; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 96. 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}; OrderedLocusNames=MG347; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71572.1; -; Genomic_DNA. DR PIR; D64238; D64238. DR RefSeq; WP_009885805.1; NZ_AAGX01000006.1. DR ProteinModelPortal; P47589; -. DR STRING; 243273.MgenG_010200001863; -. DR EnsemblBacteria; AAC71572; AAC71572; MG_347. DR KEGG; mge:MG_347; -. DR PATRIC; 20010260; VBIMycGen98045_0407. DR eggNOG; ENOG4107T6Z; Bacteria. DR eggNOG; COG0220; LUCA. DR KO; K03439; -. DR OMA; AHPEINY; -. DR OrthoDB; EOG6K6VBC; -. DR BioCyc; MGEN243273:GH2R-397-MONOMER; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-HAMAP. 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 1 210 tRNA (guanine-N(7)-)-methyltransferase. FT /FTId=PRO_0000171351. FT REGION 188 191 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01057}. FT ACT_SITE 112 112 {ECO:0000250}. FT BINDING 36 36 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 61 61 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 90 90 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 112 112 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 116 116 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01057}. FT BINDING 148 148 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01057}. SQ SEQUENCE 210 AA; 24929 MW; 5F9B0DCA113ABB26 CRC64; MRLRKVKNAL LKINQSPYFY SKDKFAKFTK KQLVLELGCG KGTFLIKEAQ KNNNFLFIGI EREPTIVLKA INKINKLDFN LENILLLCTD AKQLDDYFQA ESVQKIFINF PDPWPKKRHI QRRLTSPDFL KLFWNLLVKN GLIEFKTDND KLFEYTLTTL QENSQIFEII HQITDLNNSE FSFQNSITEY EQRFMELEIP IKKLVIKKII // ID TRUA_MYCGE Reviewed; 244 AA. AC P47428; Q49300; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=tRNA pseudouridine synthase A; DE EC=5.4.99.12; DE AltName: Full=tRNA pseudouridine(38-40) synthase; DE AltName: Full=tRNA pseudouridylate synthase I; DE AltName: Full=tRNA-uridine isomerase I; GN Name=truA; Synonyms=hisT; OrderedLocusNames=MG182; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102 AND 129-244. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in CC the anticodon stem and loop of transfer RNAs. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(38-40) = tRNA pseudouridine(38- CC 40). CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA 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; L43967; AAC71401.1; -; Genomic_DNA. DR EMBL; U02176; AAD12460.1; -; Genomic_DNA. DR EMBL; U02100; AAD12372.1; -; Genomic_DNA. DR PIR; B64220; B64220. DR RefSeq; WP_009885867.1; NZ_AAGX01000007.1. DR ProteinModelPortal; P47428; -. DR STRING; 243273.MgenG_010200002314; -. DR EnsemblBacteria; AAC71401; AAC71401; MG_182. DR KEGG; mge:MG_182; -. DR PATRIC; 20009796; VBIMycGen98045_0204. DR eggNOG; ENOG4105DI7; Bacteria. DR eggNOG; COG0101; LUCA. DR KO; K06173; -. DR OMA; YKLTIEY; -. DR OrthoDB; EOG6Z9B4R; -. DR BioCyc; MGEN243273:GH2R-191-MONOMER; -. DR Proteomes; UP000000807; 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; 1. 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 1 244 tRNA pseudouridine synthase A. FT /FTId=PRO_0000057409. FT ACT_SITE 52 52 Nucleophile. {ECO:0000250}. FT BINDING 110 110 Substrate. {ECO:0000250}. FT CONFLICT 13 13 S -> I (in Ref. 2; AAD12460). FT {ECO:0000305}. SQ SEQUENCE 244 AA; 27597 MW; AA1071218B916492 CRC64; MARYLGIVSY DGSYFKGWAI QPNLATIQGL LEQSFSLIIG RKIKVIGSGR TDKGVHAINQ TFHVDINGEI NLNLLIRKIN QLIKPHCIVK TLVLVNDSFH ARFQVKTKVY EYLINCGNLN PLQFNYVWQL NQQLDLEKLK ADATLFLGKK NFLSFSSSIH TDSIRTISKI TIQKETNQLV RLTFFGSGFL RSQVRMIVAC LVNLNTNKMA LETVAKLFEH PKKGSCVVKA PSCGLYLKTV VYEK // ID TYSY_MYCGE Reviewed; 287 AA. AC P47469; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 105. DE RecName: Full=Thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_00008}; DE Short=TS {ECO:0000255|HAMAP-Rule:MF_00008}; DE Short=TSase {ECO:0000255|HAMAP-Rule:MF_00008}; DE EC=2.1.1.45 {ECO:0000255|HAMAP-Rule:MF_00008}; GN Name=thyA {ECO:0000255|HAMAP-Rule:MF_00008}; OrderedLocusNames=MG227; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 193-287. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Provides the sole de novo source of dTMP for DNA CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP = CC dihydrofolate + dTMP. {ECO:0000255|HAMAP-Rule:MF_00008}. CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00008}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00008}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00008}. CC -!- SIMILARITY: Belongs to the thymidylate synthase family. Bacterial- CC type ThyA subfamily. {ECO:0000255|HAMAP-Rule:MF_00008}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71448.1; -; Genomic_DNA. DR EMBL; U01718; AAC43192.1; -; Unassigned_DNA. DR PIR; A64225; A64225. DR RefSeq; WP_010869385.1; NC_000908.2. DR ProteinModelPortal; P47469; -. DR EnsemblBacteria; AAC71448; AAC71448; MG_227. DR KEGG; mge:MG_227; -. DR PATRIC; 20009936; VBIMycGen98045_0264. DR KO; K00560; -. DR OMA; IVYELLW; -. DR OrthoDB; EOG6K6V53; -. DR BioCyc; MGEN243273:GH2R-249-MONOMER; -. DR UniPathway; UPA00575; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.572.10; -; 1. DR HAMAP; MF_00008; Thymidy_synth_bact; 1. DR InterPro; IPR023451; Thymidate_synth/dCMP_Mease. DR InterPro; IPR000398; Thymidylate_synthase. DR InterPro; IPR020940; Thymidylate_synthase_AS. DR Pfam; PF00303; Thymidylat_synt; 1. DR PRINTS; PR00108; THYMDSNTHASE. DR SUPFAM; SSF55831; SSF55831; 1. DR TIGRFAMs; TIGR03284; thym_sym; 1. DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; KW Nucleotide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 287 Thymidylate synthase. FT /FTId=PRO_0000140983. FT ACT_SITE 170 170 {ECO:0000255|HAMAP-Rule:MF_00008}. SQ SEQUENCE 287 AA; 33470 MW; 6BA68678A9E502D8 CRC64; MKQYLDLASY VLANGKKRKN RTDTDTLSVF GYQMKFDLTN SFPLLTTKKV NWKAIVHELL WFIKGDTNIK YLVDNGVNIW NEWPYENFKK SPSFQNETLQ EFILKVKTDN EFAKQFADLG PVYGKQWRNF NGVDQLKKVI QEIKENPNSR RLIVSSWNPS ELEKMALAPC HSLFQFYVEE DKLSLQLYQR SGDIFLGVPF NIASYALLVY LVAHETKLKP GYFIHTLGDA HIYENHIEQI KLQLTRTTLD PPQVVLKSDK SIFAYSFDDI ELVGYNYHPF IYGRVAV // ID TRXB_MYCGE Reviewed; 315 AA. AC P47348; Q49316; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 113. DE RecName: Full=Thioredoxin reductase; DE Short=TRXR; DE EC=1.8.1.9; GN Name=trxB; OrderedLocusNames=MG102; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-122. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide CC + NADPH. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P0A9P4}; CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P0A9P4}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9P4}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide CC oxidoreductase 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; L43967; AAC71320.1; -; Genomic_DNA. DR EMBL; U02197; AAD12483.1; -; Genomic_DNA. DR PIR; C64211; C64211. DR RefSeq; WP_009885660.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47348; -. DR STRING; 243273.MgenG_010200000745; -. DR EnsemblBacteria; AAC71320; AAC71320; MG_102. DR KEGG; mge:MG_102; -. DR PATRIC; 20009606; VBIMycGen98045_0112. DR eggNOG; ENOG4105C3M; Bacteria. DR eggNOG; COG0492; LUCA. DR KO; K00384; -. DR OMA; ANKFYWI; -. DR OrthoDB; EOG65XN2W; -. DR BioCyc; MGEN243273:GH2R-105-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; KW Oxidoreductase; Redox-active center; Reference proteome. FT CHAIN 1 315 Thioredoxin reductase. FT /FTId=PRO_0000166737. FT NP_BIND 45 52 FAD. {ECO:0000250|UniProtKB:P0A9P4}. FT NP_BIND 288 297 FAD. {ECO:0000250|UniProtKB:P0A9P4}. FT DISULFID 145 148 Redox-active. FT {ECO:0000250|UniProtKB:P0A9P4}. FT CONFLICT 113 122 VFSKTVIYAT -> FLAKLLSMQQ (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 315 AA; 34674 MW; 7FDF8FF755C9D424 CRC64; MLKVNADFLT KDQVIYDLVI VGAGPAGIAS AIYGKRANLN LAIIEGNTPG GKIVKTNIVE NYPGFKTITG PELGLEMYNH LLAFEPVVFY NNLIKIDHLN DTFILYLDNK TTVFSKTVIY ATGMEERKLG IEKEDYFYGK GISYCAICDA ALYKGKTVGV VGGGNSAIQE AIYLSSIAKT VHLIHRREVF RSDALLVEKL KKISNVVFHL NATVKQLIGQ EKLQTVKLAS TVDKSESEIA IDCLFPYIGF ESNNKPVLDL KLNLDQNGFI LGDENMQTNI KGFYVAGDCR SKSFRQIATA ISDGVTAVLK VRDDI // ID TYPH_MYCGE Reviewed; 421 AA. AC P47297; Q49312; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Thymidine phosphorylase; DE EC=2.4.2.4; DE AltName: Full=TdRPase; GN Name=deoA; OrderedLocusNames=MG051; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-421. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: The enzymes which catalyze the reversible phosphorolysis CC of pyrimidine nucleosides are involved in the degradation of these CC compounds and in their utilization as carbon and energy sources, CC or in the rescue of pyrimidine bases for nucleotide synthesis. CC -!- CATALYTIC ACTIVITY: Thymidine + phosphate = thymine + 2-deoxy- CC alpha-D-ribose 1-phosphate. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside CC phosphorylase 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; L43967; AAC71267.1; -; Genomic_DNA. DR EMBL; U02191; AAD12476.1; -; Genomic_DNA. DR PIR; F64205; F64205. DR RefSeq; WP_009885713.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47297; -. DR STRING; 243273.MgenG_010200001130; -. DR EnsemblBacteria; AAC71267; AAC71267; MG_051. DR KEGG; mge:MG_051; -. DR PATRIC; 20009482; VBIMycGen98045_0051. DR eggNOG; ENOG4105CMW; Bacteria. DR eggNOG; COG0213; LUCA. DR KO; K00758; -. DR OMA; VTACAGD; -. DR OrthoDB; EOG61ZTGG; -. DR BioCyc; MGEN243273:GH2R-51-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004645; F:phosphorylase activity; IEA:InterPro. DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro. DR GO; GO:0009032; F:thymidine 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; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 421 Thymidine phosphorylase. FT /FTId=PRO_0000059078. FT CONFLICT 392 392 V -> I (in Ref. 2; AAD12476). FT {ECO:0000305}. SQ SEQUENCE 421 AA; 46355 MW; 649CD517CD6E5E62 CRC64; MNIINLINKK QRGKALNLAE INWFVNAVLN KTIADYQITA FLMAIWFKGM NPNELFLLTK AMVDTGEIIK FNHHGKISVD KHSTGGIGDK VSLALVPILT SLGFSVAKLS GRGLGYTGGT IDKLEAVGVK TELTDQQAQA CLDKNDCFII GQSKDIAPVD KVLYGLRDIT GTVDSLPLIA SSIMSKKLAV MNEYIFIDLK YGKGAFCKTK KIANELAKLM QSIAKSFKRK LSVKLSDMNQ VLGKAVGNVI EVNEAVNFLK QDLDQVGQDF IDLMQTIVIN ILLETKQAKT KQKAIELYQD VLTSKKAWNR FLSFIESQGG NVELFTQKEG FFKPKYKASI KAEKSGILHF TDPIDLAKIG INLGAGRMKK TDQIDPMAGL FLMKKDNESV AVGDTVLNLY SSSPISNEYI SAAQKTIIIN K // ID UNG_MYCGE Reviewed; 245 AA. AC P47343; Q49318; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=Uracil-DNA glycosylase; DE Short=UDG; DE EC=3.2.2.27; GN Name=ung; OrderedLocusNames=MG097; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-231. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Excises uracil residues from the DNA which can arise as CC a result of misincorporation of dUMP residues by DNA polymerase or CC due to deamination of cytosine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydrolyzes single-stranded DNA or mismatched CC double-stranded DNA and polynucleotides, releasing free uracil. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase 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; L43967; AAC71315.1; -; Genomic_DNA. DR EMBL; U02201; AAD12490.1; -; Genomic_DNA. DR PIR; G64210; G64210. DR ProteinModelPortal; P47343; -. DR STRING; 243273.MgenG_010200000715; -. DR EnsemblBacteria; AAC71315; AAC71315; MG_097. DR KEGG; mge:MG_097; -. DR PATRIC; 20009596; VBIMycGen98045_0107. DR eggNOG; ENOG4105D5S; Bacteria. DR eggNOG; COG0692; LUCA. DR KO; K03648; -. DR OMA; YPAPKNI; -. DR OrthoDB; EOG6MSS63; -. DR BioCyc; MGEN243273:GH2R-100-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.470.10; -; 1. DR HAMAP; MF_00148; UDG; 1. DR InterPro; IPR018085; Ura-DNA_Glyclase_AS. DR InterPro; IPR002043; Ura_DNA_glycsylse. DR InterPro; IPR005122; Uracil-DNA_glycosylase-like. DR PANTHER; PTHR11264; PTHR11264; 1. DR Pfam; PF03167; UDG; 1. DR SMART; SM00986; UDG; 1. DR SUPFAM; SSF52141; SSF52141; 1. DR TIGRFAMs; TIGR00628; ung; 1. DR PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA damage; DNA repair; Glycosidase; KW Hydrolase; Reference proteome. FT CHAIN 1 245 Uracil-DNA glycosylase. FT /FTId=PRO_0000176115. FT ACT_SITE 72 72 Proton acceptor. {ECO:0000250}. FT CONFLICT 193 205 EHLSYPHPSPLSG -> GAFIISPSLTTKC (in Ref. FT 2). {ECO:0000305}. SQ SEQUENCE 245 AA; 28188 MW; A2EDA605D83D7CCC CRC64; MVMDDLFQRM VSCVLPSWRA FIDEEVKKPY FQALLEKLKA LKATIIPKPE LIFRVFSFFK PIDTKVIIFG QDPYPSPNDA CGLAFASNNS KTPASLKRII LRLEKEYPSL KQESSWQQNF LLNWAEQGVL LLNGILTTTV FIRNAHKNWG WEEFNCNLLT FLKNQNIKPL LVFLGVQTKN FVVKSIGNVD GFEHLSYPHP SPLSGNLFLT NPNDLFKTIN NWLKQHNQKI INWAVVKNAS FDQLS // ID UVRB_MYCGE Reviewed; 656 AA. AC P47319; Q49254; Q49446; Q49506; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 114. 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}; OrderedLocusNames=MG073; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78; 102-231 AND 414-528. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 -!- SEQUENCE CAUTION: CC Sequence=AAD10554.1; 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; L43967; AAC71291.1; -; Genomic_DNA. DR EMBL; U01743; AAD10554.1; ALT_INIT; Genomic_DNA. DR EMBL; U02119; AAD12393.1; -; Genomic_DNA. DR EMBL; U01698; AAB01010.1; -; Genomic_DNA. DR PIR; A64208; A64208. DR RefSeq; WP_010869318.1; NC_000908.2. DR ProteinModelPortal; P47319; -. DR SMR; P47319; 9-597. DR PRIDE; P47319; -. DR EnsemblBacteria; AAC71291; AAC71291; MG_073. DR KEGG; mge:MG_073; -. DR PATRIC; 20009548; VBIMycGen98045_0083. DR KO; K03702; -. DR OMA; FETKMRQ; -. DR OrthoDB; EOG6B360R; -. DR BioCyc; MGEN243273:GH2R-76-MONOMER; -. DR Proteomes; UP000000807; 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 1 656 UvrABC system protein B. FT /FTId=PRO_0000138407. FT DOMAIN 29 414 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00204}. FT DOMAIN 434 596 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_00204}. FT DOMAIN 614 649 UVR. {ECO:0000255|HAMAP-Rule:MF_00204}. FT NP_BIND 42 49 ATP. {ECO:0000255|HAMAP-Rule:MF_00204}. FT MOTIF 95 118 Beta-hairpin. FT CONFLICT 45 45 G -> A (in Ref. 2). {ECO:0000305}. FT CONFLICT 102 107 EAYLPS -> KLTYPD (in Ref. 2; AAD12393). FT {ECO:0000305}. FT CONFLICT 432 433 DN -> IT (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 656 AA; 75202 MW; 59488ADF5D283493 CRC64; MKNQTKSNSL FQLSTNYIPT GDQPEAIKKL SEFKTKQQVL LGATGTGKTF TIANVIQNSQ LPTVVIAHNK TLAGQLFNEL KQLFPKNAVE YFISYFDFYQ PEAYLPSKGI YIEKSATVNE AIKRLRVSTL HSLSTRKDVI VVGSVASIYP TSSPSDFVKY CLWFVVGKDY DLKTIKDRLV SLNYVVNKQQ LTPGKFRFQG DVLEVFPGYS DAFVIRISFF DTKVEQICQI DPLTNKILNQ LFEIKIGPAD EYVVNQSDLD IAIKNIKQEL QERVNYFNKQ NLVERAQRLA TITNHDLNDL KAWGFCSGVE NYARHLELRM ANSTPYSIFD YFKGDWLLVI DESHQTLPQL NGMYNTDLSR KQSLIDYGFR LPSALDNRPL SFAELQQKMQ KVIYVSATPR DKEISLSQNN VIEQLVRPTY LVDPIIVVKP KDNQVEDLIE EIINQRQNNT RTFVTVLTIK MAENLTEYLK ERKIKVAYIH KDIKALERLL LINDLRRGEY ECLVGINLLR EGLDVPEVAL VCIFDADIPG LPRDERSLIQ IIGRAARNEH GRVVMYANHV TEQMQKAIDE TKRRRTVQME YNKLHNKTPK TVVKPLTFVQ PIKLKAKSNA EKNAALIKQL TKEMKKAAAN QNYELAIEIR DSIFELEKEI GSKIKV // ID URK_MYCGE Reviewed; 213 AA. AC P47622; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Uridine kinase; DE EC=2.7.1.48; DE AltName: Full=Cytidine monophosphokinase; DE AltName: Full=Uridine monophosphokinase; GN Name=udk; OrderedLocusNames=MG382; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- CATALYTIC ACTIVITY: ATP + uridine = ADP + UMP. CC -!- CATALYTIC ACTIVITY: ATP + cytidine = ADP + CMP. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage CC pathway; CTP from cytidine: step 1/3. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage CC pathway; UMP from uridine: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the uridine 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; L43967; AAC71609.1; -; Genomic_DNA. DR PIR; C64242; C64242. DR RefSeq; WP_009885943.1; NZ_AAGX01000012.1. DR ProteinModelPortal; P47622; -. DR STRING; 243273.MgenG_010200002971; -. DR EnsemblBacteria; AAC71609; AAC71609; MG_382. DR KEGG; mge:MG_382; -. DR PATRIC; 20010348; VBIMycGen98045_0447. DR eggNOG; ENOG4105DBI; Bacteria. DR eggNOG; COG0572; LUCA. DR KO; K00876; -. DR OMA; HPSAFEW; -. DR OrthoDB; EOG6KMBCH; -. DR BioCyc; MGEN243273:GH2R-438-MONOMER; -. DR UniPathway; UPA00574; UER00637. DR UniPathway; UPA00579; UER00640. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro. DR GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00551; Uridine_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006083; PRK/URK. DR InterPro; IPR000764; Uridine_kinase-like. DR InterPro; IPR026008; Uridine_kinase_. DR PANTHER; PTHR10285:SF6; PTHR10285:SF6; 1. DR Pfam; PF00485; PRK; 1. DR PRINTS; PR00988; URIDINKINASE. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00235; udk; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 213 Uridine kinase. FT /FTId=PRO_0000164480. FT NP_BIND 12 19 ATP. {ECO:0000255}. SQ SEQUENCE 213 AA; 24925 MW; 33D589FB6A4A8913 CRC64; MDEKGILVAI SGGSCSGKTT VAEMIYQLLS KKLKVAIICQ DNYYKSYKNK PLLKRKTINF DHPDAFDWKL LRSHIEDLLN GSIVNVPLYD YINYTRAKKT AKIGPIDVVI LEGLMPWFDE KLSRLSKLKI FIETNGEERL IRRIERDWQR GRNIDSIIKQ WREIVAPMYE IFVEKMKRNA DLILPWSQRR EVSTSVLDVA IEHLFHKTVE KNN // ID UVRD_MYCGE Reviewed; 703 AA. AC P47486; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Probable DNA helicase II homolog; DE EC=3.6.4.12; GN Name=uvrD; OrderedLocusNames=MG244; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 277-345. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). CC -!- FUNCTION: Has both ATPase and helicase activities. Unwinds DNA CC duplexes with 3' to 5' polarity with respect to the bound strand CC and initiates unwinding most effectively when a single-stranded CC region is present. Involved in the post-incision events of CC nucleotide excision repair and methyl-directed mismatch repair (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00560}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00617}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71464.1; -; Genomic_DNA. DR EMBL; X61517; CAA43729.1; -; Genomic_DNA. DR PIR; I64226; I64226. DR RefSeq; WP_010869390.1; NC_000908.2. DR ProteinModelPortal; P47486; -. DR STRING; 243273.MgenG_010200001667; -. DR PRIDE; P47486; -. DR EnsemblBacteria; AAC71464; AAC71464; MG_244. DR KEGG; mge:MG_244; -. DR PATRIC; 20009970; VBIMycGen98045_0281. DR eggNOG; ENOG4105C4R; Bacteria. DR eggNOG; COG0210; LUCA. DR KO; K03657; -. DR OMA; IININDM; -. DR OrthoDB; EOG64N9TW; -. DR BioCyc; MGEN243273:GH2R-266-MONOMER; -. DR Proteomes; UP000000807; 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:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 3. 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; 2. DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1. DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA repair; KW DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 703 Probable DNA helicase II homolog. FT /FTId=PRO_0000102076. FT DOMAIN 1 287 UvrD-like helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00560}. FT DOMAIN 294 542 UvrD-like helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00617}. FT NP_BIND 23 28 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00560}. FT BINDING 285 285 ATP. {ECO:0000250}. SQ SEQUENCE 703 AA; 81959 MW; 14D925E1F7C6525B CRC64; MNEQQKQAIS CGKGVNVVYS GAGTGKTTII TNRFAYLVNK EKVDPSRILA ITFTKKAAKE MQFRILKLID SSLAEKTNIY TFHSFCNKFL IQTLKKRFII DDDISYFLKE FLADSKLDIN LAKQIIDNFK NTFADFEINK LDQDERLISL CEHSLLNKDE EYSTLKTQLI NAFISYEKNK ILNNKLDFHD LLIKTCNLLS NDNDLLNQWS EQFQHILVDE FQDTNQIQYE LIKMLVTKNK NLFLVGDNNQ MIYRWRGAVN GIITALKHDF NVPKSNEFFI NQNYRCDQNI LAVANQILLK IMAYEKQVKT EKNLLFSTLN SDKKPVYFQA ESVENQANWI FNKIKALNQT EKINFKDMAI LFRKNRDITT MVELIEADGT IPLPKQKSYF NQLVKLQRVL IAISTRTNLD IKRALQALKI WSNDLKELWK QSDKTNLFDF LKWSELNQKN HSSKLKATGY FNLLIKLAED QQINLLFTEL FKKLKVDQTI ENLLWKKLTE FQKDKTEFSL SEFITSLALE FDSIIENSSD TINLLTVHAA KGLEFEAVFI YGMNQGDFPL FLSQNQNDEQ HLIDELKLFY VAITRAKRFL FITAVLQINN NSIKPSSFLN YINKSEYLDI ATINYVLEQD DDFFDSTKKT DYTKKLRKES LDIIVGDLVT SRYFGKGVVV EVRDKEVLVA FKDTRYGMKW ILKNHKSLTK ALY // ID UVRC_MYCGE Reviewed; 597 AA. AC P47448; Q49305; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 95. 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}; OrderedLocusNames=MG206; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 299-383. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71424.1; -; Genomic_DNA. DR EMBL; U02182; AAD12468.1; -; Genomic_DNA. DR PIR; T09715; T09715. DR RefSeq; WP_010869373.1; NC_000908.2. DR ProteinModelPortal; P47448; -. DR EnsemblBacteria; AAC71424; AAC71424; MG_206. DR KEGG; mge:MG_206; -. DR PATRIC; 20009866; VBIMycGen98045_0238. DR KO; K03703; -. DR OMA; GAINSYK; -. DR OrthoDB; EOG6K13R9; -. DR BioCyc; MGEN243273:GH2R-215-MONOMER; -. DR Proteomes; UP000000807; 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 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; IPR004791; UvrC. DR InterPro; IPR001162; UvrC_homol_region. DR Pfam; PF01541; GIY-YIG; 1. DR Pfam; PF08459; UvrC_HhH_N; 1. DR SMART; SM00465; GIYc; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF82771; SSF82771; 1. DR TIGRFAMs; TIGR00194; uvrC; 1. DR PROSITE; PS50164; GIY_YIG; 1. DR PROSITE; PS50165; UVRC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA damage; DNA excision; DNA repair; KW Excision nuclease; Reference proteome; SOS response. FT CHAIN 1 597 UvrABC system protein C. FT /FTId=PRO_0000138317. FT DOMAIN 14 91 GIY-YIG. {ECO:0000255|HAMAP- FT Rule:MF_00203}. FT CONFLICT 370 383 HKDLAQLLNTDYIH -> QQGFSTTSKYWLYP (in Ref. FT 2). {ECO:0000305}. SQ SEQUENCE 597 AA; 68696 MW; 21DC5A69C53A475B CRC64; MTTNLKQKLK TAPKKPGCYL WKDSNGKVLY VGKASNIFNR VHQYFQKNNP YKTQLLSSQI SDVDFFILKD ENDALNLEAK LINQYQPRFN LVLKQNNGYL YFYITKAKKP TLELARKYQI KTTKCFGPFA SSKFKLREIH DLLLKLFPLR KCAPHQKNHP CFYFQMGLCM GQCMQTDTKE KYQQVISNIE QFFNDPSVVI NYLKAAEKKA SDNQEFEKAQ QFLTLQKAVL ELTKTHHTTI IKQKSSHDFI GYVFQNNVLA ITIFCYEKGE LTDKEQAVFT LEQTDIVEVE SAIITFIYHH YKTTPLPSKI TVSLDETNLK LISDSLKIGV FKPKNGNEKL ILQTVIDNAK HALATKWLKF TSNYDKTQLH KDLAQLLNTD YIHSLEIIDV SFYDQNHVVG CMLRFEDGKK IKHLSRRYNI NSLKKGDTNH IALLVYRRIL SAMQTKANLP FSDLLIIDGG KAQIKSVKQV FSLFSNVKPP IIIGLVKNKN HQTDHIMLSD FQVKKIAINS PLFHYLATIQ TEVDGFAKRS AFNKLSNHQL QNPLLQIPGV GKITAQILFD NFQTLNNIKL ASVNELSQFI KKPLAQKIKT YFAKQTD // ID UPP_MYCGE Reviewed; 206 AA. AC P47276; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 101. 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=MG030; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-206. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71246.1; -; Genomic_DNA. DR EMBL; U01773; AAD10592.1; -; Genomic_DNA. DR PIR; C64203; C64203. DR RefSeq; WP_009885912.1; NZ_AAGX01000010.1. DR ProteinModelPortal; P47276; -. DR SMR; P47276; 3-206. DR STRING; 243273.MgenG_010200002721; -. DR EnsemblBacteria; AAC71246; AAC71246; MG_030. DR KEGG; mge:MG_030; -. DR PATRIC; 20009436; VBIMycGen98045_0028. DR eggNOG; ENOG4105CZ5; Bacteria. DR eggNOG; COG0035; LUCA. DR KO; K00761; -. DR OMA; TIEGWCG; -. DR OrthoDB; EOG6HF5WX; -. DR BioCyc; MGEN243273:GH2R-30-MONOMER; -. DR UniPathway; UPA00574; UER00636. DR Proteomes; UP000000807; Chromosome. 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: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 3: Inferred from homology; KW Allosteric enzyme; Complete proteome; Glycosyltransferase; KW GTP-binding; Magnesium; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 206 Uracil phosphoribosyltransferase. FT /FTId=PRO_0000120850. FT REGION 128 136 5-phospho-alpha-D-ribose 1-diphosphate FT binding. {ECO:0000255|HAMAP- FT Rule:MF_01218}. FT REGION 196 198 Uracil binding. {ECO:0000255|HAMAP- FT Rule:MF_01218}. FT BINDING 76 76 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 101 101 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 191 191 Uracil; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 197 197 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. SQ SEQUENCE 206 AA; 22973 MW; 26B021599F8CC303 CRC64; MIKKVQHALI LNELTKLRDK NTTTSQFRMA LNQITSLLFF EATKQLPLAT VEVETPFAKT KGYKLKNDIV LVPIMRAGLG MIDAIVRYSD KIRVGHLGIY RQTQTTSVIS YYKKMPENIS DSHVIILDPM LATGTTLLTA IKSIKEDKPI KISVIAIVAA PEGINKVEKM HPHVDIFLAA IDEKLNDNRY IIPGLGDAGD RLFGTK // ID UVRA_MYCGE Reviewed; 952 AA. AC P47660; Q49295; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 114. 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}; OrderedLocusNames=MG421; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-85. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 569-668. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC71645.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAD12454.1; 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; L43967; AAC71645.1; ALT_INIT; Genomic_DNA. DR EMBL; U02172; AAD12454.1; ALT_INIT; Genomic_DNA. DR EMBL; X61514; CAA43728.1; -; Genomic_DNA. DR PIR; T09750; T09750. DR ProteinModelPortal; P47660; -. DR SMR; P47660; 9-950. DR EnsemblBacteria; AAC71645; AAC71645; MG_421. DR KEGG; mge:MG_421; -. DR PATRIC; 20010428; VBIMycGen98045_0487. DR KO; K03701; -. DR OrthoDB; EOG6QK4PS; -. DR BioCyc; MGEN243273:GH2R-475-MONOMER; -. DR Proteomes; UP000000807; 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; 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 SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00630; uvra; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA excision; KW DNA repair; DNA-binding; Excision nuclease; Metal-binding; KW Nucleotide-binding; Reference proteome; Repeat; SOS response; Zinc; KW Zinc-finger. FT CHAIN 1 952 UvrABC system protein A. FT /FTId=PRO_0000093064. FT DOMAIN 316 595 ABC transporter 1. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT DOMAIN 615 944 ABC transporter 2. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT NP_BIND 38 45 ATP. {ECO:0000255|HAMAP-Rule:MF_00205}. FT ZN_FING 259 286 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT NP_BIND 647 654 ATP. {ECO:0000255|HAMAP-Rule:MF_00205}. FT ZN_FING 746 772 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00205}. SQ SEQUENCE 952 AA; 106334 MW; FA59421690F3EB94 CRC64; MKPEWKNNDF IRVKGARENN LKNINIDIPK NQFVVITGLS GSGKSSLAFN TIYAEGRRRY LESLSSYARQ FLGNSDKPDV DLIEGLSPAI SIDQKTTSHN PRSTMGTVTE IYDYLRLLWA RIGTPYCPNG HGSIQTQTIN QIANQIFDLP NKSKVQLLAP TVKNQRGIFT NEFIKYKQLG FLRVLVDGQI YTLDDEIKLD KNTKHNISVV IDRIIINKDN QTYSRIVDSI ETIDRLTNGK IEVLKEDGTI LNFSKNHGCD KCGFSISELE PRLFSFNSPL GSCSYCKGLG FSYEPDVDKI IADSKLSINQ GAIDIFKNIV HGTSLDWQRF LSLVNHYKIP LDKPIEQLDK SQLNLILEGS DEPIEIKTIS NSGAKNIRFE HYEGIANLIK RRHLETNSQV SREWYSAYMS EITCKKCHGK KLIKDALSVK LGGIDIISFT ELSIDKSIDF LLKLELNDEQ KKIGELALKE IINRLSFLKN VGLDYLNLAR RASTLSGGEA QRIRLATQIG SQLTGVLYVM DEPSIGLHQK DNMRLIKTMM VMRDLGNTLL VVEHDSETML AADYLIDIGP KAGNEGGELV ACGTPLQVME NSNSITGQYL SGKKQISIPK NRHSGNGKTI IIKGAKVNNL KNINVTIPLN KLVLITGVSG SGKSSLINQT LVPALERILY RKGVKKDTYK EIIGANNIDK IIVVSQDPIG RTPRSNPATY ISVFDDIRDL FANTKEAKAR GYTNSRFSFN VPGGRCDKCF GDGVIRIEMH FLPDVYVKCE VCNGKKYNSQ TLEIKYLGKS IFDVLQMSCK EAYEFFKAIP NISRKLRLLC DVGLEYLQLG INVTFLSGGE AQRIKLSKFL QKKSTGKTLF VLDEPSTGLH LEDINKLLTI IQRIIKNGDT VVVIEHNLDI IKVADYIIDL GPEGGDNGGQ IVAQGTPEQL INQVNKSYTA QYLSKILKPD SI // ID Y061_MYCGE Reviewed; 461 AA. AC P47307; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Uncharacterized protein MG061; GN OrderedLocusNames=MG061; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-424. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71278.1; -; Genomic_DNA. DR EMBL; U01705; AAB01017.1; -; Genomic_DNA. DR PIR; G64206; G64206. DR STRING; 243273.MgenG_010200001200; -. DR EnsemblBacteria; AAC71278; AAC71278; MG_061. DR KEGG; mge:MG_061; -. DR PATRIC; 20009504; VBIMycGen98045_0062. DR eggNOG; ENOG4105EKN; Bacteria. DR eggNOG; COG0477; LUCA. DR OrthoDB; EOG6TTVJZ; -. DR BioCyc; MGEN243273:GH2R-63-MONOMER; -. DR Proteomes; UP000000807; 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; IPR020846; MFS_dom. DR InterPro; IPR011699; MFS_Mycoplasma. DR Pfam; PF07672; MFS_Mycoplasma; 1. DR SUPFAM; SSF103473; SSF103473; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 461 Uncharacterized protein MG061. FT /FTId=PRO_0000210404. FT TRANSMEM 87 107 Helical. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. FT TRANSMEM 158 178 Helical. {ECO:0000255}. FT TRANSMEM 215 235 Helical. {ECO:0000255}. FT TRANSMEM 257 277 Helical. {ECO:0000255}. FT TRANSMEM 299 319 Helical. {ECO:0000255}. FT TRANSMEM 320 340 Helical. {ECO:0000255}. FT TRANSMEM 356 376 Helical. {ECO:0000255}. FT TRANSMEM 397 417 Helical. {ECO:0000255}. SQ SEQUENCE 461 AA; 50972 MW; 319C4906D3E494BB CRC64; MMGIMCVCFP FLIIGDPLNG HNQLTLLRPL SDSVKTQLSS LSSNLQVGQL LGPVMINGKT MLADGTSVEL IKGLDGNSIG TAASITGYAL FIIFRSTIAI GGTTLVVYTQ PAIANLSSNR KKSILSNANL WGFNIGIAVV FTPFLFEQVQ QVASQYWVYI MTVMILVVFA NLCLFLWFES KIDHIFPQKQ TKENMSLTTQ PKSIDILKNK TTWKLIGVYG IVLILIVNPL TPAWFSILQT VSPSGSNGLI STGVYTTGLA TLAIFWVIGY ALGFVVFSPF NKTIYDKKRW MHFLLTANIV VLLIIIMFAA TLGIGSAAGF ALISIFSFIG GAFAWSLSSS NLILPYEFKD YKKNELPILF GFCWGFGYIA YTLFDITQSV FLQAPVLIQG KGTSILPGVI VSIVFFLGLI ALANLIVKFF PACWIKDGDQ LVQEMTRKWK LNEWQFVIAN KQKNRYSELL K // ID Y064_MYCGE Reviewed; 1331 AA. AC P47310; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 86. DE RecName: Full=Uncharacterized ABC transporter permease MG064; GN OrderedLocusNames=MG064; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC-4 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; L43967; AAC71282.1; -; Genomic_DNA. DR PIR; A64207; A64207. DR RefSeq; WP_010869314.1; NC_000908.2. DR EnsemblBacteria; AAC71282; AAC71282; MG_064. DR KEGG; mge:MG_064; -. DR PATRIC; 20009514; VBIMycGen98045_0066. DR KO; K02004; -. DR OMA; ITPDFMY; -. DR OrthoDB; EOG6NWBKC; -. DR BioCyc; MGEN243273:GH2R-67-MONOMER; -. DR Proteomes; UP000000807; 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 InterPro; IPR003838; ABC_permease_dom. DR Pfam; PF02687; FtsX; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 1331 Uncharacterized ABC transporter permease FT MG064. FT /FTId=PRO_0000210407. FT TRANSMEM 373 393 Helical. {ECO:0000255}. FT TRANSMEM 487 507 Helical. {ECO:0000255}. FT TRANSMEM 534 554 Helical. {ECO:0000255}. FT TRANSMEM 579 599 Helical. {ECO:0000255}. FT TRANSMEM 653 673 Helical. {ECO:0000255}. FT TRANSMEM 1206 1226 Helical. {ECO:0000255}. FT TRANSMEM 1255 1275 Helical. {ECO:0000255}. FT TRANSMEM 1297 1317 Helical. {ECO:0000255}. SQ SEQUENCE 1331 AA; 149013 MW; 899AA3E19153212C CRC64; MLNLIKNVIR SLKSAKIALI ALTFLIFVAV GGFVLLNNTV NNFNAAFNYV THTGKLSNAI INERYDFGKL EFQEQTNNSQ NSSDSFTLTL TNDSRTSFIN NALRTNPSLY EGLVTQTFSY QNKTEMTEKT NIVNQSKIIA ANNLNNALSK DKQLLVSGQL EKLNAVFREY KAINITDKSV FKKLIVSEPN DLVNSLVIFD GQNLSSSKQS DFNNFLNQFN EIKSKGKDNL STTLKTGQYQ AFLQTLFDYA QASETTLKDQ LQKLISNPDS SETNQVKNLF DTPSTLTNIG GQLTLQWTEN SLTKQIVIFD PSSYETIVAP GNWTYQQQLG KEVYPDINNW ESIKKLPLEQ FESEFLKIDQ KYKISIDNID YLVIGVGISP DFVYPVFSAS LIVPNIENEQ LYYVNQTGYE RTFSSFLTNP VETAIVARLI NLESDLNTIN QWAVENMSWP TNIKAAYSSS DTTNILNLLA ARTVFIPNLI NTINLVALFL TIAILTVAII VSILILISYL KKNTEQIGIL KANGLSGKKI NLSLLIFGLI PAIVGAISGY SFGIGFQDVA IHLFSNYWFI PTATSSFSVV GLLFFSLFVI LIMSSISLLV GSIILKKDVV KILKHDSEFK VSRLGLSSKK LFARFGIMTR FRVALAFNAP WKLVFLTLMS SFTMMILNLS FATKDSFENA QSKTNLTNQN HQYEFELASA TTQSGLLKWQ LFAELGTTDK RSESSVKLAN KRMDISNVDA SKDWKNQQVI NFLSDASGFS NDLNYLENIV QSKIGLDYSL GFNNIVSNPW RLSETLMPTN QASASNTAFQ NFLKAIITIN PSQGSQFIKQ TQDPLTKRFI YAIDSDKALK NNNEQNGSQN HLTLNDDFAK FLYSQFELIK KSGNASNEDL NAIDFENPQT IRDFYNKYNA LPPLDYKLSF NVIGLPKETI AGQIDTPKYG FLTLHGEYQN TPIKIKGIKD WKDKVDNLGP VLSDQNNHII NQELFKNYSF DPLIVNNSAA KKYQLAIGSE INIAVNNSFK RIDNKIINQD PLVNATFRVV GINNSAHDPE FFTSYSTAFK VLEYPNEWFV KKLPFNSFYA NSLLSFVQST SLFSESGIFP ATSSFSTNNT VLVELIKKTI NYKNGQMNQT SSNDSSKKEN YQKLQKALGI STDLEISKVN EYVAILARVY NGLPYNSTIS FISNVAANNA LFGNIANTTK QIQAVVIAVI IPIIMLIILL VSTTLIQELK KIAIRLKALG YSNLKILASF LSIYIPLFAF GLLISIPFSI YLIALHNEVI FASSSIFLDA FLSFESAIGS MLVLLAVLSI TFVLNWLELN KIKIDKEIKN S // ID Y029_MYCGE Reviewed; 186 AA. AC P47275; Q49223; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 75. DE RecName: Full=Uncharacterized protein MG029; GN OrderedLocusNames=MG029; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SEQUENCE CAUTION: CC Sequence=AAD10593.1; 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; L43967; AAC71245.1; -; Genomic_DNA. DR EMBL; U01773; AAD10593.1; ALT_INIT; Genomic_DNA. DR PIR; B64203; B64203. DR RefSeq; WP_009885913.1; NZ_AAGX01000010.1. DR ProteinModelPortal; P47275; -. DR STRING; 243273.MgenG_010200002726; -. DR MEROPS; C56.975; -. DR EnsemblBacteria; AAC71245; AAC71245; MG_029. DR KEGG; mge:MG_029; -. DR PATRIC; 20009434; VBIMycGen98045_0027. DR eggNOG; ENOG4107S0N; Bacteria. DR eggNOG; COG0693; LUCA. DR OMA; ANKWVIA; -. DR OrthoDB; EOG65XN5N; -. DR BioCyc; MGEN243273:GH2R-29-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR002818; DJ-1/PfpI. DR Pfam; PF01965; DJ-1_PfpI; 1. DR SUPFAM; SSF52317; SSF52317; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 186 Uncharacterized protein MG029. FT /FTId=PRO_0000210393. SQ SEQUENCE 186 AA; 20884 MW; A60F7B32027DC80E CRC64; MKKILVIVYP EMNDVEYTNV MVVFSFIKTI QTTCYHHSLK KITASNGVVE VNNIVNTINL SEFDAVYIPG GIGATKHLDK DEKLLKTINY FKVNNLYLFA ICDTPNVLFK HGIITKDEIY SSFPNPNLVM SENRSTAKVT VANKLITARS AGCALEFATV IVCTFLKDNT LNELVHKRLF GSEIKD // ID Y055_MYCGE Reviewed; 123 AA. AC P47301; Q49349; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=Uncharacterized protein MG055; GN OrderedLocusNames=MG055; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC 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; L43967; AAC71271.1; -; Genomic_DNA. DR EMBL; U02240; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A64206; A64206. DR RefSeq; WP_010869309.1; NC_000908.2. DR STRING; 243273.MgenG_010200001155; -. DR EnsemblBacteria; AAC71271; AAC71271; MG_055. DR KEGG; mge:MG_055; -. DR PATRIC; 20009490; VBIMycGen98045_0055. DR KO; K03073; -. DR OMA; IHELHRQ; -. DR OrthoDB; EOG67433G; -. DR BioCyc; MGEN243273:GH2R-55-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 InterPro; IPR005807; SecE_bac. DR TIGRFAMs; TIGR00964; secE_bact; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 123 Uncharacterized protein MG055. FT /FTId=PRO_0000210397. FT TRANSMEM 91 111 Helical. {ECO:0000255}. SQ SEQUENCE 123 AA; 14460 MW; 3EC4967DC0FFBC30 CRC64; MEKKLPFSFK KKEKLTAYDD ASIHELHKQL KLRTEAKKSK DKERTKEKEK HESLAKEKKP KLPFKKRIVN LWFGVDKEIN KIVWVKGRQL IIIFLLILLV SGLMVGIFFG INQLLITLGI FKN // ID Y060_MYCGE Reviewed; 297 AA. AC P47306; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Uncharacterized glycosyltransferase MG060; DE EC=2.4.-.-; GN OrderedLocusNames=MG060; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-241. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 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; L43967; AAC71277.1; -; Genomic_DNA. DR EMBL; U02262; AAD12528.1; -; Genomic_DNA. DR PIR; F64206; F64206. DR RefSeq; WP_010869310.1; NC_000908.2. DR ProteinModelPortal; P47306; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAC71277; AAC71277; MG_060. DR KEGG; mge:MG_060; -. DR PATRIC; 20009502; VBIMycGen98045_0061. DR OMA; ISAYHKE; -. DR OrthoDB; EOG6DRPFQ; -. DR BioCyc; MGEN243273:GH2R-62-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 297 Uncharacterized glycosyltransferase FT MG060. FT /FTId=PRO_0000059243. SQ SEQUENCE 297 AA; 35228 MW; 66CB916B3E6B7549 CRC64; MKLSVIIPTY NCASFIEKAI NSIVKNRPND LEIEVLIIDD GSIDNTNKVI KKIQDQINNL TLQYFYKSNG NWGSVINYVR NNKLAKGEWV TVLDSDDIFS KKTISIFQKY AQKQRYDAII FDYYKCWKKF LWKIPTYARF RKEIKGELKK QTPFCIPLAK FFKNEVFYQL PKLRENVGFQ DAIYTMHALQ IANNVFHVSK AGGYYFFKRV GNSMSIPWHS SRFDIEVQIC KDLIENNAQE IALVHLLRLK FRNLVDDKKI KFTVKRDFCF SGFSWYSRLI LSLMYNFWLK RYFNSSE // ID Y065_MYCGE Reviewed; 466 AA. AC P47311; Q49281; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=Putative ABC transporter ATP-binding protein MG065; GN OrderedLocusNames=MG065; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 393-466. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71283.1; -; Genomic_DNA. DR EMBL; U02154; AAD12436.1; -; Genomic_DNA. DR PIR; B64207; B64207. DR RefSeq; WP_010869315.1; NC_000908.2. DR ProteinModelPortal; P47311; -. DR STRING; 243273.MgenG_010200001250; -. DR EnsemblBacteria; AAC71283; AAC71283; MG_065. DR KEGG; mge:MG_065; -. DR PATRIC; 20009516; VBIMycGen98045_0067. DR eggNOG; ENOG4105CQU; Bacteria. DR eggNOG; COG1136; LUCA. DR KO; K02003; -. DR OMA; RENIEIG; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-68-MONOMER; -. DR Proteomes; UP000000807; 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 1 466 Putative ABC transporter ATP-binding FT protein MG065. FT /FTId=PRO_0000093239. FT DOMAIN 233 463 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 269 276 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT CONFLICT 394 399 GDEPTG -> WWWTYW (in Ref. 2; AAD12436). FT {ECO:0000305}. SQ SEQUENCE 466 AA; 54009 MW; A585044B8A90391C CRC64; MDFFSLNKII KPNQKFTSNE AEFLQIATDY LEESQNYLQK GLKQLKKEYK RSIIYNPNLE YKRFVKWKEN FTETFESYYD RFFITKYNHY SLSLLFSFIN EQIETVIASY NSFLNEHNKL AFNKVSFSFE KKLFEATQQF NNLEKNTAIS DDLPLQFKVR TTQLKAQRER ELKNLLNKIK LKNLSEKKQE ILLNNWFNSN ERLFLKNEVK KVNWLNSPRQ KQQAAQIDDQ NIIELKNVYK YITNGITTNA VLKGVDLAIK SHDFIVILGP SGSGKTTLLN IISGMDRASS GSVIVNGYNM ICLNDRKLTK FRQKYVGYIF QQYGLLPNLT VRENIEIGAN LQPDPSKRIS IDALLEAVGM DSLQKKLPNE LSGGQQQRVS IARAFAKNPL LIFGDEPTGA LDLEMTQIVL KQFLAIKKRY QTTMIIVTHN NLIANLADLV IYVADGKIKS LHRNLNPKQV EEIHWI // ID Y068_MYCGE Reviewed; 474 AA. AC P47314; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Uncharacterized lipoprotein MG068; DE Flags: Precursor; GN OrderedLocusNames=MG068; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 307-415. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; L43967; AAC71286.1; -; Genomic_DNA. DR EMBL; U02162; AAD12444.1; -; Genomic_DNA. DR PIR; E64207; E64207. DR RefSeq; WP_009885731.1; NZ_AAGX01000003.1. DR STRING; 243273.MgenG_010200001270; -. DR EnsemblBacteria; AAC71286; AAC71286; MG_068. DR KEGG; mge:MG_068; -. DR PATRIC; 20009522; VBIMycGen98045_0070. DR OMA; PAIETYK; -. DR OrthoDB; EOG6N9469; -. DR BioCyc; MGEN243273:GH2R-71-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022382; DUF31. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. DR SUPFAM; SSF50494; SSF50494; 3. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 23 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 24 474 Uncharacterized lipoprotein MG068. FT /FTId=PRO_0000018736. FT LIPID 24 24 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 24 24 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 474 AA; 54631 MW; F1BD50993842D866 CRC64; MLRRYLTLSF SSLLLLALLF LTGCSFVRPQ FRRGFRTQFK INSIPTVSDP YHINYDLTFS LNFASNKRNT YGTGWLIDWK GDENNPEKND PFKVYLATNL HVIDALRNNN DYEPYNKDSN NQAFNSEEIT RFFSIGKYTY PSIFSELNFI INAREAFVSI QTSTIPKTAY AAVNFVETQG EDESYTDSLS TDNKRDIYAD FAVIEIPLFL TNHRDYQVFN EFIKPAIETY KQLGNSSFEK KQLDQHKNDN FYMLGYPLVE SSIDALILNQ RRQYNNSYTE KYTPQTLTKD QRTIDLSREV PTLIQNKTEN STGSQLLVNQ SLSSTSEGII EFIKLPEFKL NYHNKSYRQY GRGFALQNTN FRPGSSGTLM LNNQKQIAGI YFGVLDFGED VSLMSNIGVG QILRVPQKNN TRNRSIATNK SNYDLIFGDS NTTNFYAKFA RQNNTHLYQM ISNSKDTKLK YVNTVEKTVK ASIK // ID Y119_MYCGE Reviewed; 564 AA. AC P47365; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Putative carbohydrate transport ATP-binding protein MG119; GN OrderedLocusNames=MG119; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- FUNCTION: Part of the ABC transporter complex involved in CC carbohydrates import. Probably responsible for energy coupling to CC the transport system (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. 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; L43967; AAC71337.1; -; Genomic_DNA. DR EMBL; U02149; AAD12429.1; -; Genomic_DNA. DR PIR; B64213; B64213. DR RefSeq; WP_009885675.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47365; -. DR STRING; 243273.MgenG_010200000850; -. DR EnsemblBacteria; AAC71337; AAC71337; MG_119. DR KEGG; mge:MG_119; -. DR PATRIC; 20009642; VBIMycGen98045_0130. DR eggNOG; ENOG4108JQ9; Bacteria. DR eggNOG; COG3845; LUCA. DR KO; K02056; -. DR OMA; MSIIYGF; -. DR OrthoDB; EOG6QK4RR; -. DR BioCyc; MGEN243273:GH2R-123-MONOMER; -. DR Proteomes; UP000000807; 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:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Reference proteome; Repeat; Sugar transport; KW Transport. FT CHAIN 1 564 Putative carbohydrate transport ATP- FT binding protein MG119. FT /FTId=PRO_0000092516. FT DOMAIN 6 245 ABC transporter 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT DOMAIN 315 564 ABC transporter 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 40 47 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 564 AA; 63274 MW; 4E590454A46D976E CRC64; MEKVAFKMEH ISKSFDNGKI KANVDVSLVV YENTVHTILG ENGAGKSTLT SILFGLYKPD SGKIFIGEKQ VNFKSSKDAV KHKIGMVHQH FKLIENYTVL DNIILGNESR FGFLPLINRK VSEAKIKTIM EKYGIFVDLK QKVSNLTVGQ QQRVEILKVL FRDSNILIFD EPTAVLSDLE IQNFLKIIAN FKKLGKTIVL ISHKLNEIKQ VADTATVLRL GKVVGSFDVK TTPVDKIALL MMGKELKQTK NTTDFVAKDE PVLKVQNLNL FLNKSLAYKF LVRCNNIHKA QQIKKNKPLK DLWIISFLNK LTTSNKTPKL VKGLINKLGL SYQENTDETI SFAIHKGEIF AIAGVEGNGQ SQLVNLICGI EKAASNKLIF NNIDISRWSI RKRINAGISF VLEDRHKYGL ILDQTVRFNT VNNQINNRPF SSWNFLKPME IALYSNTIIK KFDVRGSAEG SAVVRRLSGG NQQKLIIGRE MTKQNDLLVL AQVTRGLDIG AIAFIHENIL LAKANNKAIL LVSYELDEIL ALADTVAVIN KGRIVGMGKR DLMDRQSIGR LIMQ // ID Y007_MYCGE Reviewed; 254 AA. AC P47253; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 65. DE RecName: Full=Uncharacterized protein MG007; GN OrderedLocusNames=MG007; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71223.1; -; Genomic_DNA. DR PIR; G64200; G64200. DR RefSeq; WP_009885556.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47253; -. DR STRING; 243273.MgenG_010200000010; -. DR PRIDE; P47253; -. DR EnsemblBacteria; AAC71223; AAC71223; MG_007. DR KEGG; mge:MG_007; -. DR PATRIC; 20009390; VBIMycGen98045_0007. DR eggNOG; ENOG4106AK1; Bacteria. DR eggNOG; COG0470; LUCA. DR KO; K02341; -. DR OMA; INIVCTE; -. DR OrthoDB; EOG6D2KS0; -. DR BioCyc; MGEN243273:GH2R-7-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 254 Uncharacterized protein MG007. FT /FTId=PRO_0000210383. SQ SEQUENCE 254 AA; 29378 MW; 15C64F26BEC33206 CRC64; MLTTTHALLI IQRKGSFLKP FLDNYLTSIV CENKNGCKKC INCLEILNNK YNSLYWFDQI NPFKRENALQ LARIFNRERT SVNNKNIYLI EEIEKLSSNS INSLLRLVED SPINSYGIFT TKNESLILST FLSRVQKVVL KKASKVPFKV SKNDQEIITS FFTVDEQIEA IENGSFNRFK IILDACLNKK TGTEQIYHAW QIFRDFSNSE IAQLITLIIN KTENIDKKSI LFNCLKVLPY NPPKSTLFAN LVSW // ID Y010_MYCGE Reviewed; 218 AA. AC P47256; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=Uncharacterized protein MG010; GN OrderedLocusNames=MG010; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|PROSITE- CC ProRule:PRU00995}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71226.1; -; Genomic_DNA. DR PIR; A64201; A64201. DR RefSeq; WP_010869288.1; NC_000908.2. DR ProteinModelPortal; P47256; -. DR STRING; 243273.MgenG_010200003166; -. DR EnsemblBacteria; AAC71226; AAC71226; MG_010. DR KEGG; mge:MG_010; -. DR PATRIC; 20009396; VBIMycGen98045_0010. DR eggNOG; COG0358; LUCA. DR KO; K02316; -. DR OMA; YLVEGDF; -. DR OrthoDB; EOG6XDGTR; -. DR BioCyc; MGEN243273:GH2R-10-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR InterPro; IPR004611; DNA_primase-rel. DR InterPro; IPR006171; Toprim_domain. DR SMART; SM00493; TOPRIM; 1. DR TIGRFAMs; TIGR00646; MG010; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 218 Uncharacterized protein MG010. FT /FTId=PRO_0000180534. FT DOMAIN 111 193 Toprim. {ECO:0000255|PROSITE- FT ProRule:PRU00995}. SQ SEQUENCE 218 AA; 25280 MW; 71A08C5BC21B9190 CRC64; MDVRTERLNE LFFVYHKNLK NQSKSKYSRA VNYLKRRGFN LQDFLKVGGG VGYLQNKEWL NLPLYSFDGN LIGFLNRKVS YKKEFLYTPF NKPPSKSEAF VGLRELVIKD NSIYLVEGDF DWLAFRKAGI LNSLPLCGLT ISNQQVQWLK QKKIKKIFIC FDNDLAGKNG AKNLKEYLTK QGFITKVIEI KAAAKDWNDL FLLNNSNWSA VLTNQLLF // ID Y103_MYCGE Reviewed; 280 AA. AC P47349; Q49293; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Uncharacterized protein MG103; GN OrderedLocusNames=MG103; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 86-208. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71321.1; -; Genomic_DNA. DR EMBL; U02170; AAD12452.1; -; Genomic_DNA. DR PIR; D64211; D64211. DR RefSeq; WP_010869332.1; NC_000908.2. DR EnsemblBacteria; AAC71321; AAC71321; MG_103. DR KEGG; mge:MG_103; -. DR PATRIC; 20009608; VBIMycGen98045_0113. DR KO; K09762; -. DR OMA; CELRESF; -. DR OrthoDB; EOG68WR87; -. DR BioCyc; MGEN243273:GH2R-106-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR023054; Sporulation_regulator_WhiA_C. DR Pfam; PF02650; HTH_WhiA; 1. DR SUPFAM; SSF55608; SSF55608; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 280 Uncharacterized protein MG103. FT /FTId=PRO_0000210415. FT CONFLICT 86 86 L -> F (in Ref. 2; AAD12452). FT {ECO:0000305}. SQ SEQUENCE 280 AA; 32864 MW; 022BC4D71D735A2D CRC64; MTFSTQIKAE LVQNKLIDKH WNVFLAGFFQ NNLKLLYNRN WSFKVQSEAL KEQFVQNLKF DFKTKASKKY FLFEFNADIN VINTLLKLDV TTSELVVKQV YLIAAFLSGG SVSDLINSNN FHLQISSNNE FQIQQLLKLF SFFKKTVKQN QLVVYLKSYE KICNFLKLIQ AFDGYLAFEN KQLEKSFTLN QLRKSNLEVA NLMKTIRSNN QTNQLQLKSF IKSSSFAKRP LNFQRYCLIK SDHPDWSLEQ IANFFFTKYN IKISRSGIQH FSVNLKKLCQ // ID Y117_MYCGE Reviewed; 214 AA. AC P47363; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 56. DE RecName: Full=Uncharacterized protein MG117; GN OrderedLocusNames=MG117; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71335.1; -; Genomic_DNA. DR PIR; I64212; I64212. DR RefSeq; WP_010869339.1; NZ_AAGX01000002.1. DR STRING; 243273.MgenG_010200000835; -. DR EnsemblBacteria; AAC71335; AAC71335; MG_117. DR KEGG; mge:MG_117; -. DR PATRIC; 20009638; VBIMycGen98045_0128. DR eggNOG; COG1211; LUCA. DR OMA; DQITKNF; -. DR OrthoDB; EOG690MPQ; -. DR BioCyc; MGEN243273:GH2R-121-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 214 Uncharacterized protein MG117. FT /FTId=PRO_0000210421. SQ SEQUENCE 214 AA; 24952 MW; CB95ECC4F324DC55 CRC64; MDKNIFQLVQ SFAKTQNVRA NYTSQDKNIS LDFVSFETVS QSLTGFLIFN NFNKLLQLIE LIKQKQTWLY VDQLWIVDLS NNKALTDATV WIIKQEKLPV SVAAFSNQQL NQVYRNSSTS PLYLSYVKPI EVQQFFTLSP SINNNPFLNQ NPLTESPFDN NNQLFQATKS VEPSMETMEF SRFMDEFDQI TKNFSDIELE PMQFTQSFDD WSKD // ID Y125_MYCGE Reviewed; 285 AA. AC P47371; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 84. DE RecName: Full=Putative phosphatase MG125; DE EC=3.1.3.-; GN OrderedLocusNames=MG125; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof 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; L43967; AAC71343.1; -; Genomic_DNA. DR PIR; H64213; H64213. DR RefSeq; WP_010869344.1; NC_000908.2. DR ProteinModelPortal; P47371; -. DR EnsemblBacteria; AAC71343; AAC71343; MG_125. DR KEGG; mge:MG_125; -. DR PATRIC; 20009654; VBIMycGen98045_0136. DR KO; K07024; -. DR OMA; ITHHDAN; -. DR OrthoDB; EOG6B09T7; -. DR BioCyc; MGEN243273:GH2R-129-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR000150; Hypothet_cof. DR Pfam; PF08282; Hydrolase_3; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00099; Cof-subfamily; 1. DR PROSITE; PS01228; COF_1; 1. DR PROSITE; PS01229; COF_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 285 Putative phosphatase MG125. FT /FTId=PRO_0000054435. FT REGION 44 45 Phosphate binding. {ECO:0000250}. FT ACT_SITE 8 8 Nucleophile. {ECO:0000250}. FT METAL 8 8 Magnesium. {ECO:0000250}. FT METAL 10 10 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 228 228 Magnesium. {ECO:0000250}. FT METAL 229 229 Magnesium. {ECO:0000250}. FT BINDING 9 9 Phosphate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 205 205 Phosphate. {ECO:0000250}. FT BINDING 231 231 Phosphate. {ECO:0000250}. SQ SEQUENCE 285 AA; 32877 MW; 05339705CA2C49D2 CRC64; MIDLLGLDLD GTLLSKTKKI NNPSKLALTN LIAKKPSLKV MILTGRSVFS TLKHVEKLNS LFKKPIVDYF CCYGGAKLYQ IEANKPQERY KFCLENSVVE TTFSIIKKHR GLCLAYLDSY VSPYLCLAGN KLLGWFTKYF WYRKRCVFFN QNHLKQGILK ISVYFLSAKR CKKVYEILKN TFQEKVNVLS FSNNLIEITH HDANKGYAIE YMAKREQLSL NRIAVIGDSW NDYAMFKKAK YSFAMSKSPS QLKLIATNTS NKTNRYRFST LLNLISETII NQKAD // ID Y129_MYCGE Reviewed; 117 AA. AC Q49397; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Putative phosphotransferase enzyme IIB component MG129; DE EC=2.7.1.-; DE AltName: Full=Putative PTS system EIIB component; GN OrderedLocusNames=MG129; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar CC phosphotransferase system (PTS), a major carbohydrate active CC -transport system, catalyzes the phosphorylation of incoming sugar CC substrates concomitant with their translocation across the cell CC membrane. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L- CC histidine/cysteine + sugar = protein EIIB + sugar phosphate. CC {ECO:0000255|PROSITE-ProRule:PRU00421}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a CC cysteinyl or histidyl residue, depending on the transported sugar. CC Then, it transfers the phosphoryl group to the sugar substrate CC concomitantly with the sugar uptake processed by the EIIC domain. CC -!- SIMILARITY: Contains 1 PTS EIIB type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00421}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71347.1; -; Genomic_DNA. DR PIR; C64214; C64214. DR RefSeq; WP_009885683.1; NZ_AAGX01000002.1. DR ProteinModelPortal; Q49397; -. DR STRING; 243273.MgenG_010200000910; -. DR EnsemblBacteria; AAC71347; AAC71347; MG_129. DR KEGG; mge:MG_129; -. DR PATRIC; 20009662; VBIMycGen98045_0140. DR eggNOG; ENOG410748S; Bacteria. DR eggNOG; ENOG410Z51H; LUCA. DR OMA; WIVKKSK; -. DR OrthoDB; EOG6FFS9V; -. DR BioCyc; MGEN243273:GH2R-133-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 3.30.1360.60; -; 1. DR InterPro; IPR001996; PTS_IIB_1. DR SUPFAM; SSF55604; SSF55604; 1. DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Phosphoprotein; KW Phosphotransferase system; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 117 Putative phosphotransferase enzyme IIB FT component MG129. FT /FTId=PRO_0000210429. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT DOMAIN 42 117 PTS EIIB type-1. {ECO:0000255|PROSITE- FT ProRule:PRU00421}. SQ SEQUENCE 117 AA; 13457 MW; 7C1874801EB31ABF CRC64; MKWLLWLGYI FSFGLLYLWI VKKSKQIAQQ PNTKLVESTS IPFKVKDFVS ACGGKENFVN IKTTPTQLIV TFKDVNSVSL TKLNALNIKG INKNQNQFRF VLGNFVNELK KKIEDEQ // ID Y135_MYCGE Reviewed; 280 AA. AC P47381; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized protein MG135; GN OrderedLocusNames=MG135; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-260. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71352.1; -; Genomic_DNA. DR EMBL; U02114; AAD12388.1; -; Genomic_DNA. DR PIR; I64214; I64214. DR RefSeq; WP_010869348.1; NC_000908.2. DR STRING; 243273.MgenG_010200000950; -. DR EnsemblBacteria; AAC71352; AAC71352; MG_135. DR KEGG; mge:MG_135; -. DR PATRIC; 20009676; VBIMycGen98045_0147. DR OMA; ANIPTFM; -. DR OrthoDB; EOG6SJJGV; -. DR BioCyc; MGEN243273:GH2R-139-MONOMER; -. DR Proteomes; UP000000807; 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 1 280 Uncharacterized protein MG135. FT /FTId=PRO_0000210438. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 79 99 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT TRANSMEM 144 164 Helical. {ECO:0000255}. FT TRANSMEM 171 191 Helical. {ECO:0000255}. FT TRANSMEM 231 251 Helical. {ECO:0000255}. SQ SEQUENCE 280 AA; 31831 MW; 3AE6C58E57474528 CRC64; MQTLNYLVII LIIAGVISVL AFTPLVRKLK IRFYLIQVLA IVLFVYVFFG RQIIYLFPDV YGQNSQSSQN LDSLRLSRIF LLDLCPFFAV IAPVFVFLKQ KKISGVLAVF GLFGALVTLF GELIFTPVNE QDIVNFIFVG TGNNQIYFMM HFLSLLVSLA IILWDNCFSL ISFFYIHVFA LIYFSYVALM VSVFKGQITG NTTGILASDW TNGEYKNVAT FLNLSNSDPQ LVFIVGFSLS YVAILLMTLF ANIPTFMEMK KDKIFIKKEN LIRKDLELLA // ID Y014_MYCGE Reviewed; 623 AA. AC P47260; Q49343; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 111. DE RecName: Full=Putative ABC transporter ATP-binding protein MG014; GN OrderedLocusNames=MG014; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 227-333. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71230.1; -; Genomic_DNA. DR EMBL; U02235; AAA03387.1; -; Genomic_DNA. DR PIR; E64201; E64201. DR RefSeq; WP_010869290.1; NC_000908.2. DR ProteinModelPortal; P47260; -. DR STRING; 243273.MgenG_010200003141; -. DR PRIDE; P47260; -. DR EnsemblBacteria; AAC71230; AAC71230; MG_014. DR KEGG; mge:MG_014; -. DR PATRIC; 20009408; VBIMycGen98045_0014. DR eggNOG; ENOG4106NPH; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K06147; -. DR OMA; QNGIEHA; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-16-MONOMER; -. DR Proteomes; UP000000807; 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; 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 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 623 Putative ABC transporter ATP-binding FT protein MG014. FT /FTId=PRO_0000093235. FT TRANSMEM 27 47 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 81 101 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 157 177 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 181 201 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 266 286 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 307 327 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 16 325 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 365 611 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 400 407 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT CONFLICT 331 333 FNR -> LIV (in Ref. 2; AAA03387). FT {ECO:0000305}. SQ SEQUENCE 623 AA; 69537 MW; F5D46215C9A95DDB CRC64; MGLVLKEFNN KIRTALILAP FFTFAQIVID LIIPSFLASA ISVVFSIDKL KQDESGGKTI SVDFIGGANI NFANVREAQI VLATTVILLA LCGLFFGLIS IYCASYVSAN TSFLLRKKIF AKLMRITTPS HDHYGSSTLL VRLTNDVYLM EVIAFDFLRL IIRAPLLFIG GLVFAVTTNQ DMSISLLITF PLILLVIGIL NRKSIPLFKE NQKSVDKINE RVEEDVSGYK VIQSFNLHSF TNNKFKIANE GWKKNSTSSL FINSLNIPFT FFLSSLTIII ALLLVFQLDS SVSVDPLPQD AAIRPNIFAF FQYNFYIVLG FILTSLTMVN FNRSRVALGR IKDILSQPEI KTITNKDQKE LLPTLEFRNI SFGLGNKNNN NFLQNLSFKF EAYKTYGIVG PTGSGKSLIA NIIGGLYEPN EGEILIGGEK IQSIDSLYLS EMIGIVFQQN ILFKGTISSN IKIGIETRSD WKNQSDLQKN EAMKNAAKIA CADTFIEKFS DSYDHNVEQL GKNLSGGQKQ RVAIARTLIT KPRILVFDDS MSALDALTEK KVRENIENDL KLTTKIIISQ NINSIKHADK ILVIDNGRIV GFDSDQKLMK NCSLYQKMKE SQKDLGGDFD AVN // ID Y015_MYCGE Reviewed; 589 AA. AC P47261; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Putative ABC transporter ATP-binding protein MG015; GN OrderedLocusNames=MG015; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71231.1; -; Genomic_DNA. DR PIR; F64201; F64201. DR RefSeq; WP_010869291.1; NZ_AAGX01000010.1. DR ProteinModelPortal; P47261; -. DR STRING; 243273.MgenG_010200002816; -. DR EnsemblBacteria; AAC71231; AAC71231; MG_015. DR KEGG; mge:MG_015; -. DR PATRIC; 20009410; VBIMycGen98045_0015. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K06147; -. DR OMA; RIRRAFF; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-17-MONOMER; -. DR Proteomes; UP000000807; 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; 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 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 589 Putative ABC transporter ATP-binding FT protein MG015. FT /FTId=PRO_0000093237. FT TRANSMEM 9 29 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 66 86 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 161 181 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 251 271 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 280 300 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 303 323 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 9 319 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 352 586 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 385 392 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 589 AA; 66126 MW; 0EA6A816DD3A3CC9 CRC64; MEGSWSYKLL YVFLCIVLGI LYGIANPILL AQGLGFIFPI TSSNGRAVDS IYSLIYPTNL NVFIRLTIVS VTVFVAYALI FVFNVAQNYV GIKLYQQTCA TLRWKAYLKM QSMSTSFFDT QNNGDLMSRL TNDMYNIDNL FTQAGGQAIQ SLFNILTTSV LIFLLSPVIA LISLSILATL ITFSFAFLKK SKTSYSQVQN NLGDMSGYIE EVLTNHKVVH VLKLQEIMIK DFDQYNKSMI KPTVRGNTYS IFLFSWFGFI SNITYLVSIS IATAFSVNSI PSFGISVINY SFMLSYIASL RQITLALDQI FTLWNLVQLG VVSAERVFKV LDLNVEKDTA TIDKLPDIKG NIRFENVAFG YNKDKPTLTG INFSVKHGDV VAIVGPTGAG KSTIINLLMK FYKPFEGKIY MDNFEISDVT KKAWREKISI VLQDSFLFSG TIKENIRLGR QDATDDEIIA ACKTANAHDF IMRLPKGYDT YISNKADYLS VGERQLLTIA RAVIRNAPVL LLDEATSSVD VHSEKLIQES IGRLMKNKTS FIISHRLSII RDATLIMVIN DGKVLEMGNH DQLMKQNGFY ARLKQSSVR // ID Y040_MYCGE Reviewed; 591 AA. AC P47286; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Uncharacterized lipoprotein MG040; DE Flags: Precursor; GN OrderedLocusNames=MG040; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 448-517. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: To T.pallidum TmpC. {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; L43967; AAC71256.1; -; Genomic_DNA. DR EMBL; U02125; AAD12400.1; -; Genomic_DNA. DR PIR; D64204; D64204. DR RefSeq; WP_009885703.1; NZ_AAGX01000003.1. DR ProteinModelPortal; P47286; -. DR STRING; 243273.MgenG_010200001045; -. DR EnsemblBacteria; AAC71256; AAC71256; MG_040. DR KEGG; mge:MG_040; -. DR PATRIC; 20009458; VBIMycGen98045_0039. DR eggNOG; ENOG4107ID8; Bacteria. DR eggNOG; COG1744; LUCA. DR OMA; NGLWKRP; -. DR OrthoDB; EOG6H7FCZ; -. DR BioCyc; MGEN243273:GH2R-40-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR003760; Bmp. DR Pfam; PF02608; Bmp; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 30 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 31 591 Uncharacterized lipoprotein MG040. FT /FTId=PRO_0000014022. FT LIPID 31 31 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 31 31 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 591 AA; 64020 MW; 14A8FA31BB7E0928 CRC64; MGKLLFGKLV FKKSLFLLSG MSSLAVFLTA CGATKIFDSS VQLLVSDNFS TLADKSFSQM SYEGIRSFFK KSKGVDLPEA DSSQLQEGNG LWKRPGFTLS DRIATFNNIK NDGSDVIVAT GFNQQESLQA ITSDDIRFQS DKESLAKTGF IFVDGAIEKE FNKRNGVPQF KSTPTNISSV AFRSDDGSFL TGVATAVYLN LNQEYFLDKS GWSTNSSNNN ELTVSGFVGI ALPSTLSFLN GFRLGIAYFN EVIYKHLSDA QDSSAQVTTS KQTVLKQLQV ANGEKRIKKI KWISPKQGSD GETINIQDHQ SGSFSDTEPR AITIANNLID KGVNAIIPIA GPQTNLVVTQ IARRQAHTAV IGVDSAQELL DINIDAPNKD KLKMGNKKII PFSSIKALDV AVESILSTLE KGSSQNGYQG FGYNNIGTVK NNSVGVSEAG YEFLIDPVFW KNTSSMQAMS LSASLKANAA SSSDNKKKLS EVATKKNENG STKNGSNDII DKYAKLLTKS SSSTSMRNGS SDSNQQNFKT TDNDGDWTIV GDELGKYKSS ELPIFTGSSS YPTFQTEAQN VLDGGANVAS TQGFKWSFKQ I // ID Y074_MYCGE Reviewed; 137 AA. AC P47320; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 58. DE RecName: Full=Uncharacterized protein MG074; GN OrderedLocusNames=MG074; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71292.1; -; Genomic_DNA. DR PIR; B64208; B64208. DR RefSeq; WP_010869319.1; NZ_AAGX01000011.1. DR STRING; 243273.MgenG_010200002871; -. DR EnsemblBacteria; AAC71292; AAC71292; MG_074. DR KEGG; mge:MG_074; -. DR PATRIC; 20009550; VBIMycGen98045_0084. DR OMA; WFELINN; -. DR OrthoDB; EOG6130M4; -. DR BioCyc; MGEN243273:GH2R-77-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 137 Uncharacterized protein MG074. FT /FTId=PRO_0000210409. SQ SEQUENCE 137 AA; 16616 MW; 25D8FD280D3126E7 CRC64; MRQFIKLSLL VFVLLFLSEL ICRFSLRLVN SIKARYKSSV FSYTACLLFL KSFQNFSNAF QKLANWVFWF ENDVNELLSI FYFNFDQKSE KVDYNFFNGY KVTAQKVVEK EQLLTCKLSD YYRLFRDKTF WFELINN // ID Y131_MYCGE Reviewed; 74 AA. AC P47377; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 62. DE RecName: Full=Uncharacterized protein MG131; GN OrderedLocusNames=MG131; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; E64214; E64214. DR STRING; 243273.MgenG_010200000925; -. DR OMA; QYSALIP; -. DR Proteomes; UP000000807; 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 74 Uncharacterized protein MG131. FT /FTId=PRO_0000210432. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 35 55 Helical. {ECO:0000255}. SQ SEQUENCE 74 AA; 8453 MW; 5D59CFCFC6B57853 CRC64; MQYSALIPLF ILLISLVLFC FSFRKNQSEN QIVKILFFAY CIDFLALILA VMLLTFLSHG LLSLAILIPV LVFQ // ID Y133_MYCGE Reviewed; 263 AA. AC P47379; Q49489; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-MAY-2016, entry version 83. DE RecName: Full=Uncharacterized protein MG133; GN OrderedLocusNames=MG133; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-243. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC71350.1; 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; L43967; AAC71350.1; ALT_INIT; Genomic_DNA. DR EMBL; X61537; CAA43749.1; -; Genomic_DNA. DR RefSeq; WP_009885689.1; NZ_AAGX01000002.1. DR STRING; 243273.MgenG_010200000940; -. DR PRIDE; P47379; -. DR EnsemblBacteria; AAC71350; AAC71350; MG_133. DR KEGG; mge:MG_133; -. DR PATRIC; 20009672; VBIMycGen98045_0145. DR OMA; INDWNAF; -. DR OrthoDB; EOG6423CJ; -. DR BioCyc; MGEN243273:GH2R-137-MONOMER; -. DR Proteomes; UP000000807; 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; IPR011631; DUF1600. DR Pfam; PF07667; DUF1600; 1. DR PIRSF; PIRSF006834; UCP006834; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 263 Uncharacterized protein MG133. FT /FTId=PRO_0000210434. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. FT TRANSMEM 150 170 Helical. {ECO:0000255}. FT TRANSMEM 189 209 Helical. {ECO:0000255}. FT TRANSMEM 232 252 Helical. {ECO:0000255}. FT CONFLICT 236 242 IPIFASM -> SLFLHQC (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 263 AA; 31305 MW; 249E548F101060AF CRC64; MKKSIGIFYR CFYLNNKCDY YLIFLAPFSL FTQIFMVITA LISVANSGQM SLIWFTNFDT FTYQSNSLAI FLVWYYFLNH KSRWFENSSL VLSVTGYLVF TVIFFNFYAL SRFTGIVNIE PDVQGWFSTI TTQLPYSFNG SFINDWNAFS ELLLHVIHPL FYFIYVGLLF KTYKFIKPPR NLQSFLLKAG IYPSIYAFYL QTIPFLNVWD NGENSYSVYG FFTQTKYNSY VWIWSIPIFA SMFLILWMLF VINNHYYGKK HHK // ID Y037_MYCGE Reviewed; 450 AA. AC P47283; Q49463; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=Uncharacterized protein MG037; GN OrderedLocusNames=MG037; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-166. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Belongs to the NAPRTase 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; L43967; AAC71253.1; -; Genomic_DNA. DR EMBL; U01814; AAD12352.1; -; Genomic_DNA. DR PIR; A64204; A64204. DR ProteinModelPortal; P47283; -. DR STRING; 243273.MgenG_010200001010; -. DR EnsemblBacteria; AAC71253; AAC71253; MG_037. DR KEGG; mge:MG_037; -. DR PATRIC; 20009450; VBIMycGen98045_0035. DR eggNOG; ENOG41075SV; Bacteria. DR eggNOG; COG1488; LUCA. DR KO; K03462; -. DR OMA; NDHELAN; -. DR OrthoDB; EOG6P06VT; -. DR BioCyc; MGEN243273:GH2R-37-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro. DR InterPro; IPR007229; Nic_PRibTrfase-Fam. DR InterPro; IPR016471; Nicotinamide_PRibTrfase. DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C. DR PANTHER; PTHR11098; PTHR11098; 1. DR Pfam; PF04095; NAPRTase; 1. DR PIRSF; PIRSF005943; NMPRT; 1. DR SUPFAM; SSF51690; SSF51690; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 450 Uncharacterized protein MG037. FT /FTId=PRO_0000205859. FT CONFLICT 52 55 EFVW -> GVCL (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 450 AA; 51801 MW; F33E45676CA16491 CRC64; MMDKRTSEIE FHLKNLLACD AYKLSHRLMY PQDTQNLYSM LTARGVYGDF KEFVWNHDFA KEILLNVFNG FVNSVIEVKK NKLLAAALTD KLVSVFNDHE LANEFTQHIC HLASFLEKNK KMPLVAKIHE SDQSLPFRTP LITIEGVENI PNNFVWLVNY FETVLLENIW LFQTASTVAK RIKSLLEKYA KETADETSFI NFQCHDFSMR GMSSLQSALY VARAHLQYFT GSDTILGGDN SRSILASEHS VMCADGSKHE LKTFQRLLEK FKDKKLSLVI DSYDMWNVLD NIIPRLKNLI LMRGATLYLR ADSGNYQTLI CNPNYKKQDK STWAMIDYLD HHFSSTINKK GYKVLNKKIG IIYGDGITYQ KIEWILNCLK NHGYCSSNII FGVGSSTYQN LNRDTLGFVY KLTAIKRNNR WIGVKKTPIT DLSKSSKGGR YKTKRLITVY // ID Y039_MYCGE Reviewed; 384 AA. AC P47285; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 70. DE RecName: Full=Uncharacterized protein MG039; GN OrderedLocusNames=MG039; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71255.1; -; Genomic_DNA. DR PIR; C64204; C64204. DR RefSeq; WP_010869301.1; NC_000908.2. DR ProteinModelPortal; P47285; -. DR STRING; 243273.MgenG_010200001030; -. DR EnsemblBacteria; AAC71255; AAC71255; MG_039. DR KEGG; mge:MG_039; -. DR PATRIC; 20009454; VBIMycGen98045_0037. DR KO; K00111; -. DR OMA; WGVSKAN; -. DR OrthoDB; EOG6X9MHV; -. DR BioCyc; MGEN243273:GH2R-39-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF01266; DAO; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 384 Uncharacterized protein MG039. FT /FTId=PRO_0000210395. SQ SEQUENCE 384 AA; 42796 MW; 3273E860B5EE94A8 CRC64; MQTIDVLIVG GGVIGTSCAY ELSQYKLKVA LLEKNAFLGC ETSQANSGVI HSGIDPNPNK LTAKYNILGR KIWIEDWFKK LIFPRKKIAT LIVAFNNEEK LQLNLLKERG IKNSIPVENI QILDQQQTLL QEPFINPNVV ASLKVEGSWL IDPLIATKCL ALASLQNNVA IYSNKKVTKI EIDSDDDFLV FINNETTPQF KTKKLIDAAG HYADWLAETT QVDNFKQTTR KGQYLVLKNQ NNLKINTIIF MVPTIHGKGV VVAEMLDGNI LVGPNAVEGI EKNKTRSIDL DSINQIKTIG KKMVPSLQFE NSIYSFAGSR AIDIETNDFV IRTAKSNPNF IILGGMKSPG LTSSPAIAKR AVELLNLKLK KKINWNPNYN LSWI // ID Y127_MYCGE Reviewed; 145 AA. AC P47373; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Uncharacterized protein MG127; GN OrderedLocusNames=MG127; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the ArsC 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; L43967; AAC71345.1; -; Genomic_DNA. DR PIR; A64214; A64214. DR RefSeq; WP_010869345.1; NC_000908.2. DR ProteinModelPortal; P47373; -. DR STRING; 243273.MgenG_010200000900; -. DR EnsemblBacteria; AAC71345; AAC71345; MG_127. DR KEGG; mge:MG_127; -. DR PATRIC; 20009658; VBIMycGen98045_0138. DR eggNOG; COG1393; LUCA. DR KO; K16509; -. DR OMA; FITASCI; -. DR OrthoDB; EOG6WQDCS; -. DR BioCyc; MGEN243273:GH2R-131-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR006660; Arsenate_reductase-like. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR006504; Tscrpt_reg_Spx/MgsR. DR Pfam; PF03960; ArsC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR01617; arsC_related; 1. DR PROSITE; PS51353; ARSC; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 145 Uncharacterized protein MG127. FT /FTId=PRO_0000162585. SQ SEQUENCE 145 AA; 16565 MW; 1994AEAC391383C2 CRC64; MKKAGKKNSD AGKTFILISS SCSSCQKAIE FFDQNKISYV VENFYKKPIS DKRFKDILSL SEDGTESLFS KRADQIKATN SVSVEELSIS ELIKLVRERP SLLRRPIIIQ YNSSGIPKRM RIGYNSSEIK VFERKLIEPK PIIQQ // ID Y134_MYCGE Reviewed; 100 AA. AC P47380; Q49273; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=Uncharacterized protein MG134; GN OrderedLocusNames=MG134; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SEQUENCE CAUTION: CC Sequence=AAD12423.1; 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; L43967; AAC71351.1; -; Genomic_DNA. DR EMBL; U02144; AAD12423.1; ALT_INIT; Genomic_DNA. DR PIR; H64214; H64214. DR RefSeq; WP_010869347.1; NC_000908.2. DR ProteinModelPortal; P47380; -. DR STRING; 243273.MgenG_010200000945; -. DR EnsemblBacteria; AAC71351; AAC71351; MG_134. DR KEGG; mge:MG_134; -. DR PATRIC; 20009674; VBIMycGen98045_0146. DR eggNOG; COG0718; LUCA. DR KO; K09747; -. DR OrthoDB; EOG6DVJWP; -. DR BioCyc; MGEN243273:GH2R-138-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 3.30.1310.10; -; 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 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 100 Uncharacterized protein MG134. FT /FTId=PRO_0000210436. SQ SEQUENCE 100 AA; 11386 MW; C5915F63627E7BD2 CRC64; MSFKKIAEMM RQAERETKKK TLAFEQQAFE YNYKNGAIKI TILGDLTLKS INIDPVLIDA SDKVILEEMI IEATNEAVSD VKTKYDNLVE KTMPKVPGLF // ID Y141A_MYCGE Reviewed; 90 AA. AC Q2MHT0; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 13-APR-2016, entry version 45. DE RecName: Full=Uncharacterized protein MG141.1; GN OrderedLocusNames=MG141.1; ORFNames=MG_477; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; ABC59633.1; -; Genomic_DNA. DR RefSeq; WP_009885828.1; NZ_AAGX01000007.1. DR ProteinModelPortal; Q2MHT0; -. DR EnsemblBacteria; ABC59633; ABC59633; MG_477. DR KEGG; mge:MG_477; -. DR PATRIC; 20009712; VBIMycGen98045_0162. DR OMA; ERESDVK; -. DR OrthoDB; EOG6TN4DN; -. DR BioCyc; MGEN243273:GH2R-149-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 3.30.1230.10; -; 1. DR InterPro; IPR007393; DUF448. DR Pfam; PF04296; DUF448; 1. DR SUPFAM; SSF64376; SSF64376; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 90 Uncharacterized protein MG141.1. FT /FTId=PRO_0000234017. SQ SEQUENCE 90 AA; 10473 MW; 4F1EB39897D2885A CRC64; MQLITRLCLL TRKHFVKREL LRLVKLDNQL EIDLNQNLKG RGYYLSVFGL KLDKKHLKAV VEKHLKVSCN DAKLTAMITA LQQLAQDEKK // ID Y147_MYCGE Reviewed; 375 AA. AC P47393; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 76. DE RecName: Full=Uncharacterized protein MG147; GN OrderedLocusNames=MG147; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71365.1; -; Genomic_DNA. DR PIR; C64216; C64216. DR EnsemblBacteria; AAC71365; AAC71365; MG_147. DR KEGG; mge:MG_147; -. DR PATRIC; 20009724; VBIMycGen98045_0168. DR OrthoDB; EOG6MD92G; -. DR BioCyc; MGEN243273:GH2R-155-MONOMER; -. DR Proteomes; UP000000807; 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 1 375 Uncharacterized protein MG147. FT /FTId=PRO_0000210442. FT TRANSMEM 21 41 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 161 181 Helical. {ECO:0000255}. FT TRANSMEM 203 223 Helical. {ECO:0000255}. FT TRANSMEM 234 254 Helical. {ECO:0000255}. FT TRANSMEM 289 309 Helical. {ECO:0000255}. FT TRANSMEM 338 358 Helical. {ECO:0000255}. SQ SEQUENCE 375 AA; 43189 MW; A14AF07D574E8046 CRC64; MLLLRALFLE LKTNKNCKAL LLLLIPLLVG LTLIIYGIVL FSTEGVIDHG DHNHLRARFQ LTLEEIIVFV VGSIILFFTL ASFCVSCFML MRSPKQKQLE VDHANKTNLK PKAIVNCDLF QLGDYCVFTF KKLSFKQRFK QDFFARSKFS FRSELYRLCL VGVLIALNLA LSLIEIPGIV LPWGSSIQFR FFNTAILFIA VRLVGLLSTS LVALITPWLH LLIHPIHTPI SSLFYMVNDF LVLWIFYFFF FHLFKAEVNQ TTTVVDNKPF SQLVNTKKTK WTKFFSLLVI SFLCGFIEGL GFYFGYFLIL GNVSSLGLKI YYDGLQQRDL INSSNVLFFL MTTTAIFSIK YIFEMLFFFS VEKNVVNIAN HFGLY // ID Y148_MYCGE Reviewed; 409 AA. AC P47394; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 63. DE RecName: Full=Uncharacterized protein MG148; GN OrderedLocusNames=MG148; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71366.1; -; Genomic_DNA. DR PIR; D64216; D64216. DR RefSeq; WP_010869355.1; NC_000908.2. DR EnsemblBacteria; AAC71366; AAC71366; MG_148. DR KEGG; mge:MG_148; -. DR PATRIC; 20009726; VBIMycGen98045_0169. DR OMA; INDQKQE; -. DR OrthoDB; EOG6CP3W2; -. DR BioCyc; MGEN243273:GH2R-156-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR InterPro; IPR019219; DUF2130. DR Pfam; PF09903; DUF2130; 1. DR PIRSF; PIRSF005850; UCP005850; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 409 Uncharacterized protein MG148. FT /FTId=PRO_0000210444. SQ SEQUENCE 409 AA; 48520 MW; 64A686361ED5998D CRC64; MKYVKVQIIN KSTIELLEDA KKGEKINLDL INQVDQTNIL NTITTNQKLA WEKELSAQFI NQQNELIKNF EIEIIKLKTM LNDKEQALLL KTKLELQNQF QKQIENYINE INKLKLTNKE LEITNQKQLE SSLKLQRNEF EEKINQQNLT IEKLKIQQAR SSIWAVAKKG NELEKWCENQ YESYADSFEN CQFTRYKTEI NLLDENDFPN EKADYIFSFF GEKTNKIPFL SICCEMKSEF NDSKHKSKNK DHISKLVRDA KRANCKYAFL ISELELETEN DIQVRLMPTL ESGVEVYLVR PMFFILMLKL FYKLAKKLFA LNRFQSVELI DKNKLNEQFK QLKDNFLTKT FLEIEKVCKS NLVDIETLEK AVVKLRVRNE RVLDQLLNKW TKKIDSFDLQ LTKKITNNY // ID Y149_MYCGE Reviewed; 281 AA. AC P47395; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 74. DE RecName: Full=Uncharacterized lipoprotein MG149; DE Flags: Precursor; GN OrderedLocusNames=MG149; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71367.1; -; Genomic_DNA. DR PIR; E64216; E64216. DR RefSeq; WP_010869356.1; NZ_AAGX01000007.1. DR STRING; 243273.MgenG_010200002119; -. DR EnsemblBacteria; AAC71367; AAC71367; MG_149. DR KEGG; mge:MG_149; -. DR PATRIC; 20009728; VBIMycGen98045_0170. DR OMA; NGETHEH; -. DR OrthoDB; EOG60KNCV; -. DR BioCyc; MGEN243273:GH2R-157-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 23 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 24 281 Uncharacterized lipoprotein MG149. FT /FTId=PRO_0000014028. FT LIPID 24 24 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 24 24 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 281 AA; 32428 MW; AB8628BEADD005FF CRC64; MKLYRSLKAA LLPGICTSIL LASCASTNTY QDQRNALISL ASNRDTLIAN AKKSKEEVQK EVTKMNSSTS SMMTATQSVA ITTHQTTEKT NNSKYDLDKL FKDYILYVVD NFSGLVFKRT GGHRIQLIDK DKEILDGGNL TKHTHHDHNH MHNHEHEHEE HHDEEETEVV GRALSFTNGI FLVIDYKKDS ERKNMSGSTT MMHQHHHEAE EHKEERKLSL NLKAYKFNTP FNISEFISAW HHKESHNSDT EFNNLHNKYD KEELDIIDYN FEEKAVDETI A // ID Y011_MYCGE Reviewed; 287 AA. AC P47257; Q49362; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=Uncharacterized protein MG011; GN OrderedLocusNames=MG011; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-255. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71227.1; -; Genomic_DNA. DR EMBL; U02257; AAD12522.1; -; Genomic_DNA. DR PIR; B64201; B64201. DR RefSeq; WP_009885973.1; NZ_AAGX01000015.1. DR ProteinModelPortal; P47257; -. DR STRING; 243273.MgenG_010200003161; -. DR EnsemblBacteria; AAC71227; AAC71227; MG_011. DR KEGG; mge:MG_011; -. DR PATRIC; 20009398; VBIMycGen98045_0011. DR eggNOG; COG0189; LUCA. DR OMA; VEYRAYI; -. DR OrthoDB; EOG6N9493; -. DR BioCyc; MGEN243273:GH2R-11-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013651; ATP-grasp_RimK-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR Pfam; PF08443; RimK; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 287 Uncharacterized protein MG011. FT /FTId=PRO_0000210385. FT DOMAIN 115 287 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT CONFLICT 158 158 T -> P (in Ref. 2; AAD12522). FT {ECO:0000305}. FT CONFLICT 255 255 A -> R (in Ref. 2; AAD12522). FT {ECO:0000305}. SQ SEQUENCE 287 AA; 33433 MW; 9AFCCFAA6B814B28 CRC64; MGKIKLKNRK ALVVYDNKDD FEKNQTFALS LIKELQKKKL NAEVLLLENK DINFEAKINE AELILNRSRK VDFLKTNNQI NTFLVNPFNV VFIANDKYET YKWLKQNRFL TVNSSLLSKE TIKSFPVIVK KRNSHGGKDV HLVNSADEIK HLNIENATEW IVQPFLSIGT VEYRAYILFG KIIKVIKKIS NANQFKANFS QGAEVSLFKL KWFTKRKIKK IAKRLREGYY AIDFFLNRYN RVIVNEIEDA AGARALVQLC PDLNITKIII RTIISKFKKF LKKKLIS // ID Y018_MYCGE Reviewed; 1031 AA. AC P47264; P47262; P47263; Q49209; Q49302; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 3. DT 13-APR-2016, entry version 98. DE RecName: Full=Uncharacterized ATP-dependent helicase MG018; DE EC=3.6.4.-; GN OrderedLocusNames=MG018; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 640-740 AND 802-902. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC -!- SIMILARITY: Contains 1 SWIM-type zinc finger. CC {ECO:0000255|PROSITE-ProRule:PRU00325}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71234.2; -; Genomic_DNA. DR EMBL; U02179; AAD12465.1; -; Genomic_DNA. DR EMBL; U01757; AAD10571.1; -; Genomic_DNA. DR PIR; G64201; G64201. DR PIR; H64201; H64201. DR PIR; T09676; T09676. DR RefSeq; WP_010869292.1; NC_000908.2. DR ProteinModelPortal; P47264; -. DR STRING; 243273.MgenG_010200002801; -. DR EnsemblBacteria; AAC71234; AAC71234; MG_018. DR KEGG; mge:MG_018; -. DR PATRIC; 20009412; VBIMycGen98045_0016. DR OMA; VYRIIAK; -. DR OrthoDB; EOG64R61X; -. DR BioCyc; MGEN243273:GH2R-18-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000330; SNF2_N. DR InterPro; IPR007527; Znf_SWIM. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00176; SNF2_N; 1. DR Pfam; PF04434; SWIM; 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. DR PROSITE; PS50966; ZF_SWIM; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; Metal-binding; KW Nucleotide-binding; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1 1031 Uncharacterized ATP-dependent helicase FT MG018. FT /FTId=PRO_0000074380. FT DOMAIN 590 751 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 868 1022 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT ZN_FING 50 85 SWIM-type. {ECO:0000255|PROSITE- FT ProRule:PRU00325}. FT NP_BIND 603 610 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 702 705 DEAQ box. FT CONFLICT 893 893 D -> S (in Ref. 3; AAD10571). FT {ECO:0000305}. SQ SEQUENCE 1031 AA; 119737 MW; DD83F049B64B3A39 CRC64; MTVAEIKKLA LNNQVFNEAK ALLEKGNVIF PKKFLKRKKI IIEVLDGKVF KVQINLKTAA AHLDCSCSND KQNCVHIIAA LLKYNDLKNQ DNKEFDLNKA DKLECKEVEI LIENVSLAIV NGSWKLKIGF VINIDKVQTN TTALRFYCCD NKDVYFLHTE DEQLFRIALD KFNSVERQTL LIFDQLNKTK QMQYENNSLL FNLDQFLSLV KEVKKPSLFL LNEDKTDNIL FLRSQHKING LSHVCGFLNN KVFDFVSYNE KTKQIVLRLA YLNKFTDFKF PYNINIYKLA FGETLFFHFL IHLKMNGFKN IFFQSDVVIV KESEYLPKMF LTIEFNTQKN KFITDAFFKY KNKNSNTLTT VYPHRYYLAQ KTNTSNFNRL LFYEQALQRF YEELFQIDYL RRFENIPIKD KNQIALFKTV FDDYKTIDLA ELKLTSNLLN YKQLHFSISD IKALKIEDRQ LKIEFKAGGI DLKLIKSVLS NYYKGNAICI GEDGWYDLND ENAKALISFW SQIDLRNATC DANNNLLLAK YHLFEVVDTI SKYTDVTNLL DEKTALQLKI ASENQFHLSL DNNQINNLRK YQKEGVKWIR ALEDNQFGGI LADEMGLGKT AQVIFAMLDS YQSTKSLLPS LIIVPASLLL NWKSEFQKFA PHVKIVTANG NFKERSQVYE SLKNQILLMS FNVLRSDIKW ISQKKFHYVV IDEAQGIKNE NSTVTKAAKK IKGNFCLALT GTPIENRLLD LWSCFDFVLP NFLGNKKQFS DQFEKEKNDE SFQKLMKKTS PFILRRTKNK VLKELPKKII TDIYVELSEE HQKLYDKQKT DGLKEIKESD AKNALNILSL ILKLRHICSL VKDNDVNDFE DNSKANAALN IIYEALENKR KVILFTQFLD VIDCFKQTLK NQKIDHLVFD GRKTVKNRNT IIQKFNSAKE PCVMLASLKA GGVGINLTAA EVVIHFDVWW NSAVENQATD RAHRIGQSKT VQVYRIIAKN TIEERVCQVQ NQKQELVKKT LVEDVNFFKS LSHEELLKLF E // ID Y027_MYCGE Reviewed; 151 AA. AC P47273; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=Uncharacterized protein MG027; GN OrderedLocusNames=MG027; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71243.1; -; Genomic_DNA. DR PIR; I64202; I64202. DR PDB; 1Q8C; X-ray; 2.00 A; A=1-151. DR PDBsum; 1Q8C; -. DR ProteinModelPortal; P47273; -. DR SMR; P47273; 12-151. DR STRING; 243273.MgenG_010200002736; -. DR EnsemblBacteria; AAC71243; AAC71243; MG_027. DR KEGG; mge:MG_027; -. DR PATRIC; 20009430; VBIMycGen98045_0025. DR eggNOG; COG0781; LUCA. DR OMA; ALLIMDH; -. DR OrthoDB; EOG6S7XWB; -. DR BioCyc; MGEN243273:GH2R-27-MONOMER; -. DR EvolutionaryTrace; P47273; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.940.10; -; 1. DR InterPro; IPR015268; DUF1948. DR InterPro; IPR006027; NusB_RsmB_TIM44. DR Pfam; PF09185; DUF1948; 1. DR SUPFAM; SSF48013; SSF48013; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 151 Uncharacterized protein MG027. FT /FTId=PRO_0000210389. FT HELIX 14 28 {ECO:0000244|PDB:1Q8C}. FT HELIX 29 31 {ECO:0000244|PDB:1Q8C}. FT HELIX 36 45 {ECO:0000244|PDB:1Q8C}. FT TURN 49 51 {ECO:0000244|PDB:1Q8C}. FT HELIX 55 81 {ECO:0000244|PDB:1Q8C}. FT HELIX 100 116 {ECO:0000244|PDB:1Q8C}. FT HELIX 120 133 {ECO:0000244|PDB:1Q8C}. FT TURN 145 147 {ECO:0000244|PDB:1Q8C}. SQ SEQUENCE 151 AA; 17480 MW; 8F3266E3CF16EE32 CRC64; MAITVKGLTN KLTRTQRRIA VVEFIFSLLF FLPKEAEVIQ ADFLEYDTKE RQLNEWQKLI VKAFSENIFS FQKKIEEQQL KNQLEIQTKY NKISGKKIDL LTTAVVLCAL SEQKAHNTDK PLLISEALLI MDHYSQGAEK KQTHALLDKL L // ID Y028_MYCGE Reviewed; 201 AA. AC P47274; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 74. DE RecName: Full=Uncharacterized protein MG028; GN OrderedLocusNames=MG028; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71244.1; -; Genomic_DNA. DR PIR; A64203; A64203. DR RefSeq; WP_009885914.1; NZ_AAGX01000010.1. DR EnsemblBacteria; AAC71244; AAC71244; MG_028. DR KEGG; mge:MG_028; -. DR PATRIC; 20009432; VBIMycGen98045_0026. DR OMA; ISIGMSK; -. DR OrthoDB; EOG62RSFG; -. DR BioCyc; MGEN243273:GH2R-28-MONOMER; -. DR Proteomes; UP000000807; 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 1 201 Uncharacterized protein MG028. FT /FTId=PRO_0000210391. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. SQ SEQUENCE 201 AA; 23238 MW; 2D69E5E6F1BFAEA1 CRC64; MKRNWRQHYN VFLANLVLVF GFALNILVAK QSLNNTTPQF RFLFVTPFLG VVIGAVLYFF DVKWFLIDYP YKKFHFQKKW AIVYLSGVIV FFLNVLIGVV LLVVMVNYIT NQILEREYER LFTNSLPYLW STTGTSIVLS LISIGMSKTA HFFIDIEILK AKKGEPTDPN KTDNRAVVIN LDENKKNEKE QSPPSAEMTS L // ID Y032_MYCGE Reviewed; 666 AA. AC P47278; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 64. DE RecName: Full=Uncharacterized protein MG032; GN OrderedLocusNames=MG032; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; L43967; AAC71248.1; -; Genomic_DNA. DR PIR; E64203; E64203. DR RefSeq; WP_010869297.1; NC_000908.2. DR EnsemblBacteria; AAC71248; AAC71248; MG_032. DR KEGG; mge:MG_032; -. DR PATRIC; 20009440; VBIMycGen98045_0030. DR OMA; LHNLERQ; -. DR OrthoDB; EOG6Z0QJK; -. DR BioCyc; MGEN243273:GH2R-32-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 666 Uncharacterized protein MG032. FT /FTId=PRO_0000215244. SQ SEQUENCE 666 AA; 77303 MW; D703C107A8E2AB7F CRC64; MKTIHKLFLG LCLPATLGPL LGIVVTNTDQ SIKFTSKSNS INKNNQNKEL ALLRDNLMNE AKVDEPLSFE KRFENFKNKY SDIHSLNNSV FSLHDVYDLL GGFKQSLTTF FDEVIAQQQK IKDADKIFPS TKDNPPKEEN PNVLDTLANY QGAGFFPSLG KNGFNLPEAV FQNFTDFRIN DYKIKNFNVD LVSENDIIKH DKVRYAFEVK FNIALVLSIN KSNVDFDFDF ILKTDNFSDI ENFNEIFNRK PALQFRFYTK INVHKLSFNG SDSTYIANIL LQDQFNLLEI DLNKSIYALD LENAKERFDK EFVQPLYQKR REAKLAWEEE QRRIAEEQRR QEEERARILK ELKEKAEKDK RVKEAQNNLQ KALGNLDTFF NFFSSGQDRV LLGFDPNKYN VQTREGLFKA LQISYSNFKT WTFYISLLGW KEGSVKLLKK PIWNALRDDK AFQYAFGLGP NTSEQQLGRV TLPGYGYEGI RMSDWLRWAL GYYTSFTLSP PKNVEANLIG DANDKKHIWI SPHTFKLNRE YGDGERFKGK AYRFKLSISF ELEGHLTAHW WTIAFRGSIP GSWSGKLRVT HEFDGDVPYY RLHTTPPQYR LTDDMKLLFV PHSIQRVTAV GNESINGLLR SQNLHNLERQ SYEATAPIDL ISYMLYAISD KKPPQK // ID Y045_MYCGE Reviewed; 483 AA. AC P47291; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=Uncharacterized lipoprotein MG045; DE Flags: Precursor; GN OrderedLocusNames=MG045; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-127. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71261.1; -; Genomic_DNA. DR EMBL; U02166; AAD12448.1; -; Genomic_DNA. DR PIR; I64204; I64204. DR RefSeq; WP_010869305.1; NC_000908.2. DR ProteinModelPortal; P47291; -. DR STRING; 243273.MgenG_010200001090; -. DR EnsemblBacteria; AAC71261; AAC71261; MG_045. DR KEGG; mge:MG_045; -. DR PATRIC; 20009468; VBIMycGen98045_0044. DR eggNOG; ENOG4107HJJ; Bacteria. DR eggNOG; COG0687; LUCA. DR KO; K11069; -. DR OMA; HEVEISD; -. DR OrthoDB; EOG6S7XQ8; -. DR BioCyc; MGEN243273:GH2R-45-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR000044; Uncharacterised_lipoprot_MG045. DR PRINTS; PR00905; MG045FAMILY. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 483 Uncharacterized lipoprotein MG045. FT /FTId=PRO_0000014024. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 483 AA; 54876 MW; 899D4CB60D78F69B CRC64; MKKQLKYCFF SLFVSLSSIL SSCGSTTFVL ANFESYISPL LLERVQEKHP LTFLTYPSNE KLINGFANNT YSVAVASTYA VSELIERDLL SPIDWSQFNL KKSSSSSDKV NNASDAKDLF IDSIKEISQQ TKDSKNNELL HWAVPYFLQN LVFVYRGEKI SELEQENVSW TDVIKAIVKH KDRFNDNRLV FIDDARTIFS LANIVNTNNN SADVNPKEDG IGYFTNVYES FQRLGLTKSN LDSIFVNSDS NIVINELASG RRQGGIVYNG DAVYAALGGD LRDELSEEQI PDGNNFHIVQ PKISPVALDL LVINKQQSNF QKEAHEIIFD LALDGADQTK EQLIKTDEEL GTDDEDFYLK GAMQNFSYVN YVSPLKVISD PSTGIVSSKK NNAEMKSKQM STDQMTSEKE FDYYTETLKA LLEKEDSAEL NENEKKLVET IKKAYTIEKD SSIRWNQLVE KPISPLQRSN LSLSWLDFKL HWW // ID Y055B_MYCGE Reviewed; 127 AA. AC Q9ZB81; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 74. DE RecName: Full=Uncharacterized protein MG055.2; GN OrderedLocusNames=MG055.2; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. 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; L43967; AAC71281.1; -; Genomic_DNA. DR RefSeq; WP_009885720.1; NZ_AAGX01000003.1. DR STRING; 243273.MgenG_010200001165; -. DR EnsemblBacteria; AAC71281; AAC71281; MG_474. DR KEGG; mge:MG_474; -. DR PATRIC; 20009492; VBIMycGen98045_0056. DR OMA; INTACEN; -. DR OrthoDB; EOG6RZBD3; -. DR BioCyc; MGEN243273:GH2R-57-MONOMER; -. DR Proteomes; UP000000807; 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 1 127 Uncharacterized protein MG055.2. FT /FTId=PRO_0000210399. FT TRANSMEM 13 35 Helical. {ECO:0000255}. FT TRANSMEM 57 81 Helical. {ECO:0000255}. SQ SEQUENCE 127 AA; 14631 MW; 4F00F3E6726D5ECF CRC64; MKVFKKLHNL NEILLLISIF FLVCIISLVG IGIIFDLIRK ASLSAIRSDP IFFNLRAVLI VLGVFAICFM IIQLVISIMI WKTINTACEN IEPKFKKILH WSCFLPFGLL QLYCYQKIKL VKQADNL // ID Y075_MYCGE Reviewed; 1024 AA. AC P47321; Q49190; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=Uncharacterized protein MG075; GN OrderedLocusNames=MG075; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156; 269-402; 643-736 AND RP 808-947. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC43189.1; 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; L43967; AAC71293.1; -; Genomic_DNA. DR EMBL; U01715; AAC43189.1; ALT_INIT; Unassigned_DNA. DR EMBL; U02251; AAD12514.1; -; Genomic_DNA. DR EMBL; U01749; AAD10562.1; -; Genomic_DNA. DR EMBL; U01775; AAD10595.1; -; Genomic_DNA. DR PIR; C64208; C64208. DR RefSeq; WP_010869320.1; NZ_AAGX01000011.1. DR STRING; 243273.MgenG_010200002876; -. DR PRIDE; P47321; -. DR EnsemblBacteria; AAC71293; AAC71293; MG_075. DR KEGG; mge:MG_075; -. DR PATRIC; 20009552; VBIMycGen98045_0085. DR OMA; LITEMIY; -. DR OrthoDB; EOG68H83X; -. DR BioCyc; MGEN243273:GH2R-78-MONOMER; -. DR Proteomes; UP000000807; 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 1024 Uncharacterized protein MG075. FT /FTId=PRO_0000210411. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 951 971 Helical. {ECO:0000255}. SQ SEQUENCE 1024 AA; 116425 MW; 5B1540E6855CB554 CRC64; MKLSTITTIC LSISGAFGTT AIALPTTVAL LKNHQQQNTE KQQNPIKDIR FGLNNVQVPN TIPLHQTVVE VTNNKAIVDY KDAPQKFFLA KSALNNKLQV EFDKFLLRTG VINALNADLK EWIDQTLFIP NQSFFDLSAN KLNLTLSNQS EVSLDLEFIF TNFSDKNQPL KLPFDGSVVV NANESYTYSV KATLQKLKVL TYSRADHSVG ISYAIPTVSL NGKTQNDFSF NPFKSNINFA FKNVYNALNP FEAQQYLVGQ GKFLNQKVNA DDVKNDINNH IETQFNVAKI TATLLGKAFK QFGEHKNGQP LSLLKVLSGL NNEFKQLFNY VRPGLGDFVS DLIQSSSQSS NKKTVYQLLF ENKTTIIHLL QDLNISELNS VLPVVDILFE GINSAESLYQ RIQSFKDLIV PALKADKQLK SLEAIILAVL DNPNTYVFDL VYQNKSILFN LLSDFLKNTA NTLPFLQEQF DIVNHLFANE AIFDLFSNAD FVEKIADLFL AKQKVQEVNN DGTKSTKIVD SILVATLKGL VGDQLSSITE LLNIYIFENE FLNRNDSNSS VKKQQTDSLK NLFSVIGDIL SETNVNKITL HAVKNNELLS LVETASTLKI KHLNVQYKVL VDKFELKNSF IKELLNFFPD TKDITPTIKK VLFESENYKT LRKKYENEGF PGYHWAKFIV PGTFNSAENT FYSAIDKTKS IRDLFADMLF GKSLESVNDS DSFIKINGSF TLKYHGDNLN LLPNYHSLIT KNVGYQIVNV NFHIDARLLT AELQNTVFSN PKPVIKSPVE LSKSLFEVWK TIFENSVNQI LKKEYTFKDN LKFFPFKADG SSRLEFDLSK PDQRVIPFAF VDGYQFQLKK ELIPNKETKK EANSSPVLKL YDAVKRNDRQ YRPNHHHDDL RNYPSLKSQL ELILNLGDKL KANNDFIDDT VVNALQYKTS FKSTLKVNSL GIPINLFFFT LWLKFNLEIP IDGSLTLTSV NVVFPYSLYD TSSNEFTRIV DRLNFTDTNF YLKDAFPNFW FVGF // ID Y116_MYCGE Reviewed; 251 AA. AC P47362; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 65. DE RecName: Full=Uncharacterized protein MG116; GN OrderedLocusNames=MG116; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71334.1; -; Genomic_DNA. DR EMBL; U02127; AAD12404.1; -; Genomic_DNA. DR PIR; H64212; H64212. DR RefSeq; WP_010869338.1; NC_000908.2. DR ProteinModelPortal; P47362; -. DR STRING; 243273.MgenG_010200000835; -. DR EnsemblBacteria; AAC71334; AAC71334; MG_116. DR KEGG; mge:MG_116; -. DR PATRIC; 20009636; VBIMycGen98045_0127. DR eggNOG; COG1211; LUCA. DR OMA; FILIEAN; -. DR OrthoDB; EOG6B3662; -. DR BioCyc; MGEN243273:GH2R-120-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:InterPro. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001228; IspD. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF01128; IspD; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 251 Uncharacterized protein MG116. FT /FTId=PRO_0000210419. SQ SEQUENCE 251 AA; 29020 MW; 65B5A033AE551765 CRC64; MKRTLNIGIV LCENFLSDQQ NAVDSYTQVY EDVRMFEFGL KLFQSLPFNI QETLIFCNAE QHKIVDKAAK KYKNTTVFFS RDTDVANVYE AKVFIQEKYK LTQDYKKRGV SSYYDSCCFI LIEANRPLTA IKTVKSVYEK ALIEKAAIAV LPYNGTLMNG NNDVVFSHLQ DKNRFNYWKQ SKAYEVQYPQ AYTLNKLNQF SKQQFLRARS MLDLMKISNK SPLSIVDGSA YAFRVVTNLD FEILLGILKN G // ID Y123_MYCGE Reviewed; 471 AA. AC P47369; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 69. DE RecName: Full=Uncharacterized protein MG123; GN OrderedLocusNames=MG123; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 413-471. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC 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; L43967; AAC71341.1; -; Genomic_DNA. DR EMBL; U01796; AAD12322.1; -; Genomic_DNA. DR PIR; F64213; F64213. DR RefSeq; WP_010869342.1; NC_000908.2. DR EnsemblBacteria; AAC71341; AAC71341; MG_123. DR KEGG; mge:MG_123; -. DR PATRIC; 20009650; VBIMycGen98045_0134. DR OMA; YFKQVCD; -. DR OrthoDB; EOG60654R; -. DR BioCyc; MGEN243273:GH2R-127-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 471 Uncharacterized protein MG123. FT /FTId=PRO_0000210427. FT TRANSMEM 10 30 Helical. {ECO:0000255}. SQ SEQUENCE 471 AA; 55082 MW; C0917A8C477410CA CRC64; MLLNLNNNSV LIVAFVIVSL FFLIIVGFAL NLAIAFSLHL KQNKNNKKYI LNDQQIQLRL TEKQAQLTTL LNFYQQKIES VNREKSWLES QLQVIDKKDL KQAQKLTLHL KKDQILAQLN EKLIQKKVDQ PLVNELQKTK LSYLERLVDQ KIKLSENNFK SAFLKTKVKE TAFNIFAAKN KVNWEYFKQV CDADCTLKNL EDEVEITFSN WSYLRRMQAL LAFEKLISKI KTVKINELVI NETLDEVKNE ISQTAFQAGE KIVKEFQITN LNEQITRLIG LQKYYFGTDQ LNLLELAVLT TKLVILLNKK FKLDLDLELL KAASLFNYLK WVDNNQFFQI LNTKLNQLLI SDQVIAIIQQ QELSFYPDQY GMLINGVKTM IREHNTIDFE KLVFLNSTKL IDNFYLYDLN MIHAVEYNNC FYYFVSVKPF EIKSLAELDL FVVLLKTFLA KKQKQNPKAV KLFITTKILA I // ID Y146_MYCGE Reviewed; 424 AA. AC Q49399; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=UPF0053 protein MG146; DE AltName: Full=VXpSPT7_orf424; GN OrderedLocusNames=MG146; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0053 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC -!- SIMILARITY: Contains 1 DUF21 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; L43967; AAC71364.1; -; Genomic_DNA. DR PIR; B64216; B64216. DR RefSeq; WP_010869353.1; NC_000908.2. DR ProteinModelPortal; Q49399; -. DR EnsemblBacteria; AAC71364; AAC71364; MG_146. DR KEGG; mge:MG_146; -. DR PATRIC; 20009722; VBIMycGen98045_0167. DR OMA; HHETSII; -. DR OrthoDB; EOG64FKB6; -. DR BioCyc; MGEN243273:GH2R-154-MONOMER; -. DR Proteomes; UP000000807; 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; IPR000644; CBS_dom. DR InterPro; IPR002550; DUF21. DR Pfam; PF00571; CBS; 2. DR Pfam; PF01595; DUF21; 1. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix. FT CHAIN 1 424 UPF0053 protein MG146. FT /FTId=PRO_0000088378. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 71 91 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT DOMAIN 14 190 DUF21. FT DOMAIN 210 270 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 272 332 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 424 AA; 48720 MW; A361AAE5B995DA87 CRC64; MDSAPSGLTL TVIILSIILL AFISTVVSAY ETAITSLTPY RWKNYIKTNN KQDKLSTKII NHFQNHYSSC LITILITNNI VAIMVSNILF LALEQTIKNE LLSSVLNLVV SGVLIVSFCE ILPKTLGRIN VIRTLVLFAY LVYFFYLIFW PITKLTSLIL KKYENPLPVS RKDVYYFIDE IEQNGLFSKE DSLLIKKTLI FDQVLVKKVM IKWKKVAYCY LNDSINLIAK QFLQRQFSRM PVVDKTTNKI VGFIHLKDFF TAKEANPKSL DLNQLLYPVV LVQDSTPIKQ ALRQMRLNRA HLAVVNDKHE KTIGIVSMED IIEELVGEIY DEHDDIQPIQ VLDENVWLVL PNVKAAYFFN KWIKPDLVKS KNITIQHYLA SLDNDSFACQ NKLDTPLFSV EVIADSEDKT KILYEIRKKS DVIA // ID Y202_MYCGE Reviewed; 122 AA. AC P47444; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 57. DE RecName: Full=Uncharacterized protein MG202; GN OrderedLocusNames=MG202; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71420.1; -; Genomic_DNA. DR PIR; C64222; C64222. DR RefSeq; WP_010869370.1; NC_000908.2. DR STRING; 243273.MgenG_010200001347; -. DR EnsemblBacteria; AAC71420; AAC71420; MG_202. DR KEGG; mge:MG_202; -. DR PATRIC; 20009856; VBIMycGen98045_0234. DR OMA; AISEDHY; -. DR OrthoDB; EOG66QM68; -. DR BioCyc; MGEN243273:GH2R-210-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 122 Uncharacterized protein MG202. FT /FTId=PRO_0000210452. SQ SEQUENCE 122 AA; 13513 MW; F3391BB7EEC794C5 CRC64; MSEQKRRTIQ IAISEDHYEE LQKALELLKG TQLPFSTTVE QFVELILSNY VATSNKISSL AKSGFDVASL QQELEKIGNL SGVDDNLKGF LSELLKTSRN GFSNPNKDGK KNDDDNNSSS KS // ID Y009_MYCGE Reviewed; 262 AA. AC P47255; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Uncharacterized metal-dependent hydrolase MG009 {ECO:0000305}; DE EC=3.1.-.- {ECO:0000305}; GN OrderedLocusNames=MG009; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:P0AFQ7}; CC Note=Binds 2 divalent metal cations per subunit. CC {ECO:0000250|UniProtKB:P0AFQ7}; CC -!- SIMILARITY: Belongs to the TatD-type hydrolase 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; L43967; AAC71225.1; -; Genomic_DNA. DR PIR; I64200; I64200. DR RefSeq; WP_009885976.1; NZ_AAGX01000015.1. DR ProteinModelPortal; P47255; -. DR STRING; 243273.MgenG_010200003176; -. DR EnsemblBacteria; AAC71225; AAC71225; MG_009. DR KEGG; mge:MG_009; -. DR PATRIC; 20009394; VBIMycGen98045_0009. DR eggNOG; ENOG4105F8V; Bacteria. DR eggNOG; COG0084; LUCA. DR KO; K03424; -. DR OMA; RGKRNRP; -. DR OrthoDB; EOG66QM1C; -. DR BioCyc; MGEN243273:GH2R-9-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR018228; DNase_TatD-rel_CS. 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. DR PROSITE; PS01137; TATD_1; 1. DR PROSITE; PS01091; TATD_3; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome. FT CHAIN 1 262 Uncharacterized metal-dependent hydrolase FT MG009. FT /FTId=PRO_0000202006. FT METAL 7 7 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 9 9 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 96 96 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 96 96 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 132 132 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 156 156 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 211 211 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. SQ SEQUENCE 262 AA; 30373 MW; B8AC017F78C7FA18 CRC64; MEYFDAHCHL NCEPLLSEIE KSIANFKLIN LKANVVGTDL DNSKIAVELA KKYPDLLKAT IGIHPNDVHL VDFKKTKKQL NELLINNRNF ISCIGEYGFD YHYTTEFIEL QNKFFEMQFE IAETNKLVHM LHIRDAHEKI YEILTRLKPT QPVIFHCFSQ DINIAKKLLS LKDLNIDIFF SIPGIVTFKN AQALHEALKI IPSELLLSET DSPWLTPSPF RGKVNWPEYV VHTVSTVAEI KKIEIAEMKR IIVKNAKKLF WH // ID Y012_MYCGE Reviewed; 287 AA. AC P47258; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized protein MG012; GN OrderedLocusNames=MG012; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71228.1; -; Genomic_DNA. DR RefSeq; WP_010869289.1; NC_000908.2. DR ProteinModelPortal; P47258; -. DR EnsemblBacteria; AAC71228; AAC71228; MG_012. DR KEGG; mge:MG_012; -. DR PATRIC; 20009400; VBIMycGen98045_0012. DR KO; K05844; -. DR OMA; NIALARW; -. DR OrthoDB; EOG6DZDX8; -. DR BioCyc; MGEN243273:GH2R-12-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013651; ATP-grasp_RimK-type. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX. DR Pfam; PF08443; RimK; 1. DR TIGRFAMs; TIGR00768; rimK_fam; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 287 Uncharacterized protein MG012. FT /FTId=PRO_0000205506. FT DOMAIN 115 287 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT NP_BIND 178 188 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT METAL 248 248 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 261 261 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 261 261 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 263 263 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT BINDING 145 145 ATP. {ECO:0000255}. SQ SEQUENCE 287 AA; 32733 MW; 7A14AF52A5AD7BBD CRC64; MKKINVVYNP AFNPISSKLN QTQLLKNASE ELDIELKFFT SFDINTTKAK ANLPFISNKI LFMDKNIALA RWLESNGFEV INSSIGINNA DNKGLSHAII AQYPFIKQIK TLLGPQNFDR EWNPVMLDVF INQIKQSMEF PVIVKSVFGS FGDYVFLCLD EQKLRKTLMS FNQQAIVQKY ITCSKGESVR VIVVNNKVIG ALHTTNNSDF RSNLNKGAKA ERFFLNKEQE NLAVKISKVM QLFYCGIDFL FDQDRSLIFC EVNPNVQLTR SSMYLNTNLA IELLKAI // ID Y025_MYCGE Reviewed; 298 AA. AC P47271; Q49359; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Uncharacterized glycosyltransferase MG025; DE EC=2.4.-.-; GN OrderedLocusNames=MG025; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 172-298. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 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; L43967; AAC71241.1; -; Genomic_DNA. DR EMBL; U02253; AAD12517.1; -; Genomic_DNA. DR PIR; G64202; G64202. DR ProteinModelPortal; P47271; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAC71241; AAC71241; MG_025. DR KEGG; mge:MG_025; -. DR PATRIC; 20009426; VBIMycGen98045_0023. DR OMA; PAYTWLP; -. DR OrthoDB; EOG6HXJ6D; -. DR BioCyc; MGEN243273:GH2R-25-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 298 Uncharacterized glycosyltransferase FT MG025. FT /FTId=PRO_0000059241. FT CONFLICT 200 201 EP -> DA (in Ref. 2; AAD12517). FT {ECO:0000305}. SQ SEQUENCE 298 AA; 35044 MW; B7BCCC73EB2CA023 CRC64; MPSKYLFTVI IPTYNCCQYI KKALDSLLLQ NEYFLKTQVL IVNDGSLDNT KEVVSDYLIK YSNISYFEKT NGNWGSVINY VKKNKLALGQ YITVLDSDDY FLKDSFKKVA RFFGHDMIIG AFYCYINENK TRFLKPYFGK TGVIKEHTKL RTPHSQPIAK FYSNKLFYEL HDLKEKLFFQ DCLMYHDAIN RVESVFYLRE PLAVWFSTRP GNSTTTSWEN PNKFNAWCEI LQKMNLYGAG IVIYIYTMLP GFLKQLKKKQ LILNLNHKPA YTWLPKPLAF IFGGLMAFKT RKYIKYPK // ID Y098_MYCGE Reviewed; 477 AA. AC P47344; Q49231; Q49509; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Uncharacterized protein MG098; GN OrderedLocusNames=MG098; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-155 AND 278-382. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GatC 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; L43967; AAC71316.1; -; Genomic_DNA. DR EMBL; U01701; AAB01013.1; -; Genomic_DNA. DR EMBL; U01782; AAD12771.1; -; Genomic_DNA. DR PIR; H64210; H64210. DR RefSeq; WP_009885655.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47344; -. DR STRING; 243273.MgenG_010200000720; -. DR EnsemblBacteria; AAC71316; AAC71316; MG_098. DR KEGG; mge:MG_098; -. DR PATRIC; 20009598; VBIMycGen98045_0108. DR eggNOG; ENOG4107IE5; Bacteria. DR eggNOG; COG0721; LUCA. DR OMA; IFSAIIE; -. DR OrthoDB; EOG6Q2SJC; -. DR BioCyc; MGEN243273:GH2R-101-MONOMER; -. DR Proteomes; UP000000807; 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:0006450; P:regulation of translational fidelity; IEA:InterPro. DR InterPro; IPR003837; Asp/Glu-ADT_csu. DR Pfam; PF02686; Glu-tRNAGln; 1. DR SUPFAM; SSF141000; SSF141000; 1. DR TIGRFAMs; TIGR00135; gatC; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 477 Uncharacterized protein MG098. FT /FTId=PRO_0000105363. FT TRANSMEM 23 43 Helical. {ECO:0000255}. FT TRANSMEM 61 81 Helical. {ECO:0000255}. FT TRANSMEM 108 128 Helical. {ECO:0000255}. FT TRANSMEM 131 151 Helical. {ECO:0000255}. FT TRANSMEM 171 191 Helical. {ECO:0000255}. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT TRANSMEM 285 305 Helical. {ECO:0000255}. FT TRANSMEM 326 346 Helical. {ECO:0000255}. FT CONFLICT 87 87 F -> V (in Ref. 2; AAB01013). FT {ECO:0000305}. FT CONFLICT 372 382 DMQSLIMPNVI -> EYAKLNYAQCY (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 477 AA; 54046 MW; 3FCCDD95A2C35684 CRC64; MGEIKNTAPT SDISTSGFIY FAVVFLIIIV YLFFKNILFL FFFKRYPKNT PKIGVSNITT IAMIIAVAVS VVLVLMALAG GLTAALFRGY PGFRVTLELI LVKISGLLFG PIIGIFSAAT IDFLTVIFSG GVFNIGYVLG AILTGMIAGI LREVLISTSF LNNKTLSDFA YLVLSVGMVF ASFLVTQFFV ISVTQNLSAF QSNDQIVLRF NASPLNFSIS LQRYVQIIFY FAMVVIITMV VLYFVWIIKQ KHFNYAYSKF FFRRYKHANH QFTLFVLTKE NWFYLILNVI TLATTSLLMI NIAFIPIFDT QTTGQTYDFW LLVRLLFAPL IFLLDIIVIY PILLLLTPIM LKGFKTVASE TQTKGIKKSF SDMQSLIMPN VISHKKQQLI RKEMQQLAKT IRIDLSDKEV DALVEEFKEI TKSFNKVTKI DTTNVQPMYA PFEFSPTPLR KDKPVVDKHA KQLLNNCCEV KTGFVKV // ID Y184_MYCGE Reviewed; 317 AA. AC Q49400; Q49252; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=Uncharacterized adenine-specific methylase MG184; DE EC=2.1.1.72; DE AltName: Full=M.MgeORF184P; GN OrderedLocusNames=MG184; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 174-240. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S- CC adenosyl-L-homocysteine + DNA 6-methylaminopurine. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-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; L43967; AAC71403.1; -; Genomic_DNA. DR EMBL; U02115; AAD12389.1; -; Genomic_DNA. DR PIR; D64220; D64220. DR RefSeq; WP_010869363.1; NC_000908.2. DR REBASE; 78740; M.MgeORF184P. DR EnsemblBacteria; AAC71403; AAC71403; MG_184. DR KEGG; mge:MG_184; -. DR PATRIC; 20009800; VBIMycGen98045_0206. DR KO; K00571; -. DR OMA; PNNCLWL; -. DR OrthoDB; EOG60CWHX; -. DR BioCyc; MGEN243273:GH2R-193-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR025247; EcoRI_methylase. DR Pfam; PF13651; EcoRI_methylase; 2. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 317 Uncharacterized adenine-specific FT methylase MG184. FT /FTId=PRO_0000088015. SQ SEQUENCE 317 AA; 37053 MW; 7CBF45151ACD0B57 CRC64; MHHFNRAKKA KNNEFFTLID EIENEVINYQ KQFANKTIFC NCNDGKNSHF FQFFQTNFNQ LQLKKLIGFS FNNLSQADKF TFDGNKVTKT KLKGNGDFSS DESIEVLKQA DIVVTNPPFS LFQSFIDLLI QHNKQFLVLG LNAAVSYNHI FTYFKTNKLW FGYTVNKTMS FSVNSDYQLY NPKTSNFFTK NGKCFQKIAG ISWFTNLGKP HYNPFLNTNC FYKNNEKNYP KFDWYDAIYV NKIKNIPMDW NGLMGVPLTF LNCYNPKQFE LVDCLANPYA TLDTLKTNAF VKLNQGDVRN VNGKRRYVRV IIKKQQI // ID Y188_MYCGE Reviewed; 329 AA. AC P47434; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Probable ABC transporter permease protein MG188; GN OrderedLocusNames=MG188; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Probably part of a binding-protein-dependent transport CC system. Probably responsible for the translocation of the CC substrate across the membrane. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. MalFG subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71407.1; -; Genomic_DNA. DR PIR; H64220; H64220. DR RefSeq; WP_009886002.1; NZ_AAGX01000020.1. DR ProteinModelPortal; P47434; -. DR STRING; 243273.MgenG_010200003338; -. DR EnsemblBacteria; AAC71407; AAC71407; MG_188. DR KEGG; mge:MG_188; -. DR PATRIC; 20009818; VBIMycGen98045_0215. DR eggNOG; ENOG4107Z33; Bacteria. DR eggNOG; COG1175; LUCA. DR KO; K02025; -. DR OMA; IFAALWP; -. DR OrthoDB; EOG625K13; -. DR BioCyc; MGEN243273:GH2R-197-MONOMER; -. DR Proteomes; UP000000807; 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 Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 329 Probable ABC transporter permease protein FT MG188. FT /FTId=PRO_0000060285. FT TRANSMEM 30 50 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 96 116 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 128 148 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 176 196 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 234 254 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 283 303 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 88 303 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 329 AA; 37201 MW; 45BFB75ACE8BAE25 CRC64; MFKWLLKHHN QPHSLQLGLL DQPLPFWKPF LLFLPALLTT ILFTIIPFFL SLQKGFSANS DLYDLSSQSF SLRTFQDLFS ESNFVLGLRN SFLYSLISLP FSIIIAIVIA SAIVFVYKKL LRGFWQTVFF LPYVTSGVAI SIAFVYIFDS ASGILNTVFN VNTKWLDSGS RDTFNALWAI LIFGVWKNLA FNVLIISTAM LSVNPQLYKV ASLDSANPVR QFFKITLPSI RPTLIFLTTL LILGGMQVFP LALFENKPEE AVANGGNSIL LYIFQQIQSG NTNLAGAATL VLFVLGVCYG LVLRNGFYLI EWLQWKIKQL YVQKQLTLY // ID Y189_MYCGE Reviewed; 318 AA. AC P47435; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 95. DE RecName: Full=Probable ABC transporter permease protein MG189; GN OrderedLocusNames=MG189; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Probably part of a binding-protein-dependent transport CC system. Probably responsible for the translocation of the CC substrate across the membrane. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. MalFG subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC71408.1; 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; L43967; AAC71408.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_009886003.1; NZ_AAGX01000020.1. DR ProteinModelPortal; P47435; -. DR STRING; 243273.MgenG_010200003343; -. DR EnsemblBacteria; AAC71408; AAC71408; MG_189. DR KEGG; mge:MG_189; -. DR PATRIC; 20009820; VBIMycGen98045_0216. DR eggNOG; ENOG4105DR3; Bacteria. DR eggNOG; COG0395; LUCA. DR KO; K02026; -. DR OMA; KIDITAY; -. DR OrthoDB; EOG6GR3D7; -. DR BioCyc; MGEN243273:GH2R-198-MONOMER; -. DR Proteomes; UP000000807; 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 Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 318 Probable ABC transporter permease protein FT MG189. FT /FTId=PRO_0000060287. FT TRANSMEM 42 62 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 98 118 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 134 154 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 169 189 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 230 250 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 282 302 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 99 301 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 318 AA; 36540 MW; 567552D0348CED85 CRC64; MFKNNLRFTS WINQHKFYQL DLSLKTRSIK QIVLTLVFKT LVLGFFGLIV IFPFYLMVVV SFASDERALD TRTPILWPDS WNFDNFSRVL SDGKYLNAIV VNTLVTVLSV LLTLFFTICM GYSFSLRKWK YKKLVWFFFL SVLILPESAL LIGQYRIVIV ANWNNPNSPL IVLGLIMPFV SSVFSGFMYR TSFEAIPSQL KESALIDGCN GFNYFLKIAL PMVKSTSWTV GILTAFSAWN SYLWPLLLLG NRVDLNINLW VLQQGILDAN SSDEQIRTLL NLKMSAAILA ILPMFIIYFL FHKRIMNAIK NRANTIKG // ID Y208_MYCGE Reviewed; 196 AA. AC P47450; Q49234; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 72. DE RecName: Full=Uncharacterized protein MG208; GN OrderedLocusNames=MG208; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 55-183. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71426.1; -; Genomic_DNA. DR EMBL; U01785; AAD10606.1; -; Genomic_DNA. DR PIR; I64222; I64222. DR RefSeq; WP_009885745.1; NZ_AAGX01000004.1. DR ProteinModelPortal; P47450; -. DR STRING; 243273.MgenG_010200001392; -. DR EnsemblBacteria; AAC71426; AAC71426; MG_208. DR KEGG; mge:MG_208; -. DR PATRIC; 20009870; VBIMycGen98045_0240. DR eggNOG; ENOG4107HHA; Bacteria. DR eggNOG; COG1214; LUCA. DR OMA; FVKLCKA; -. DR OrthoDB; EOG647TXQ; -. DR BioCyc; MGEN243273:GH2R-217-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro. DR InterPro; IPR022496; T6A_YeaZ. DR TIGRFAMs; TIGR03725; T6A_YeaZ; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 196 Uncharacterized protein MG208. FT /FTId=PRO_0000210454. FT CONFLICT 180 183 IEDP -> TKIL (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 196 AA; 22535 MW; FA4FD18361F4E7FE CRC64; MFFLSKYKLF LDCAYKTLNI IILEMKTNAV VDELSIGVEQ NLTELAVYYL ETMLTKNKLK KSSIKQFYVT IGPGSFTGQR IATIIAKSWC LLYPSCELYA LNSLRFQIPY EHGISKISCG NDQNYCGLYS QTTSEIKLIS KADFVKLCKA NNELPMYENF ENIESYSKLL LSNIDHFERI EDPLTLQPIY LKDPVN // ID Y242_MYCGE Reviewed; 630 AA. AC P47484; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 76. DE RecName: Full=Uncharacterized protein MG242; GN OrderedLocusNames=MG242; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-295. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71463.1; -; Genomic_DNA. DR EMBL; U02194; AAD12480.1; -; Genomic_DNA. DR PIR; G64226; G64226. DR RefSeq; WP_010869389.1; NC_000908.2. DR ProteinModelPortal; P47484; -. DR EnsemblBacteria; AAC71463; AAC71463; MG_242. DR KEGG; mge:MG_242; -. DR PATRIC; 20009966; VBIMycGen98045_0279. DR OMA; WIINDIE; -. DR OrthoDB; EOG6K13P2; -. DR BioCyc; MGEN243273:GH2R-264-MONOMER; -. DR Proteomes; UP000000807; 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 1 630 Uncharacterized protein MG242. FT /FTId=PRO_0000210481. FT TRANSMEM 254 274 Helical. {ECO:0000255}. FT TRANSMEM 504 524 Helical. {ECO:0000255}. FT TRANSMEM 564 584 Helical. {ECO:0000255}. FT TRANSMEM 601 621 Helical. {ECO:0000255}. SQ SEQUENCE 630 AA; 74235 MW; 6A4C2A91D706D6B9 CRC64; MKFNKLNLSH CISFYISEVS EVFFESINQH PSRDFVNNIL QKIKTTLSEE ELEKLNSIEE VTKDEKIVIM LNHVLKKIVS KTGSSKCDLF NVIKQDRFNS PVYIQSINAF ENNLINNEFA ERRYDYLIEV NKNSYLKKFV NSIRISFFLD LRAQILSGSF TLNLVNKSIE KQKKTEIFKD IFVNALVKHF ICNQLYPISL NSFIFDSENP SNKLALKERI KLLKTNWNSL FFDKFYNCLN NKNKQQLQET SDEMFYAVIN TYLIMLISVE ELRVYFTSKE PALILKVLDK KNTLREDPDQ NPETDLYELI QFIEQNYLKK DKKTSWNKKK VQDLEQLLEE INKINLETKN ESLAYPDEIT ELEIDNDNFV STKQVFRNQL ELQLLHGIVI NPEKYGIGMW SSYFADWSEY KNLIEQMLNP KSGNDFYQFE KDIDESICQI NKKYLTFISS DSNTFLIVKN DDVKVISNYV WAQLFFETRR WIINDIEFDL YEKGFDKSHF SRNIALLESL SFSWLDPFYG LTSIKEIMQK IDSKSNLKTS IEEMVNRFKH EQRINKKDNE RVLMIFAYIA AFVVGFINFF SMVFTILTVS DLNAGLTVPN IIVISIASVL AFILIVIAVL FRFKWKHIKH // ID Y243_MYCGE Reviewed; 226 AA. AC P47485; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 2. DT 13-APR-2016, entry version 65. DE RecName: Full=Uncharacterized protein MG243; GN OrderedLocusNames=MG243; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 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; L43967; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; H64226; H64226. DR RefSeq; WP_014894004.1; NC_000908.2. DR STRING; 243273.MgenG_010200001662; -. DR OMA; HELFLWV; -. DR Proteomes; UP000000807; 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; IPR010432; RDD. DR Pfam; PF06271; RDD; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 226 Uncharacterized protein MG243. FT /FTId=PRO_0000210483. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. SQ SEQUENCE 226 AA; 26257 MW; B1F5653433CADB9F CRC64; MQIKVINETN KTVQIFQCAK VKHRALAWLC DVFLLAIVLV VIFLITQAFS DNRFLLFLVL SCSQTILWTV YFIFLPFFWD GKTLFRNLLK IKLFAFDKRF LRIMIHELFL WILLSVLFLV IASYFFINQN SSEALNFFTN LDKPNAIAIT IRTITILISF LQLIFIGYFC FSSEKQALQE ILSNTFMVQE KHTLKSKPTS LKTNNQPDPA NLPGVIALDE VEKLIN // ID Y268_MYCGE Reviewed; 228 AA. AC P47510; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 78. DE RecName: Full=Uncharacterized protein MG268; GN OrderedLocusNames=MG268; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71490.1; -; Genomic_DNA. DR PIR; F64229; F64229. DR RefSeq; WP_009885899.1; NZ_AAGX01000009.1. DR ProteinModelPortal; P47510; -. DR STRING; 243273.MgenG_010200002619; -. DR EnsemblBacteria; AAC71490; AAC71490; MG_268. DR KEGG; mge:MG_268; -. DR PATRIC; 20010034; VBIMycGen98045_0309. DR eggNOG; ENOG41088X7; Bacteria. DR eggNOG; COG1428; LUCA. DR OMA; YIVENHS; -. DR OrthoDB; EOG6423DZ; -. DR BioCyc; MGEN243273:GH2R-295-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0019206; F:nucleoside kinase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002624; DCK/DGK. DR InterPro; IPR031314; DNK_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01712; dNK; 1. DR PIRSF; PIRSF000705; DNK; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 228 Uncharacterized protein MG268. FT /FTId=PRO_0000210496. FT NP_BIND 21 28 ATP. {ECO:0000255}. SQ SEQUENCE 228 AA; 26892 MW; 7DF7206D4EB6A99D CRC64; MQLKKPHFQP NKIANCIVIG GMIALGKTTI ANTLANHIQA AKVVCELETN DQLVELLLAK MYERSDELLY SPLFQLYFTL NRFGKYQNNC NTINPTIFDR SIFEDWLFAK HNIIRPAVFS YYNQLWNRLA KELVNKHGVP NLYVILDGDW KLFEKRLFMR NRKVEIDNFT KNQLYFQNLH RVYTGFMEAV CNDFGINYCI IDAKLPIVTI IKMILEKLKL QKLDWKFI // ID Y303_MYCGE Reviewed; 357 AA. AC P47545; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Putative ABC transporter ATP-binding protein MG303; GN OrderedLocusNames=MG303; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71525.1; -; Genomic_DNA. DR PIR; E64233; E64233. DR RefSeq; WP_010869419.1; NC_000908.2. DR ProteinModelPortal; P47545; -. DR STRING; 243273.MgenG_010200002504; -. DR EnsemblBacteria; AAC71525; AAC71525; MG_303. DR KEGG; mge:MG_303; -. DR PATRIC; 20010136; VBIMycGen98045_0354. DR eggNOG; ENOG4105C1C; Bacteria. DR eggNOG; COG1122; LUCA. DR KO; K16787; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-339-MONOMER; -. DR Proteomes; UP000000807; 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; 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 357 Putative ABC transporter ATP-binding FT protein MG303. FT /FTId=PRO_0000093243. FT DOMAIN 72 312 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 107 114 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 357 AA; 40786 MW; AFB1012F886E090E CRC64; MQTPQIKLDL IEQKYHLQAQ KANLKLAKLD SKKLFSFYKK VDKIINPFYF LNSKKSIPFF NSKLLNIEQD PLFFNNISVF VNKHNDGQII KCCSGVIEPN KITVIFGESG SGKTTLIKQL GLFEKPSFGY INCANYCYFA NQYQQKITKN FKQKIGYILQ KAEDQFFCDS ILEEVLTGAV NLKLCHKKDV NYAKKYLDLC GLENIPLIKN PIELSDGQKK RLALASVLAM QVKFLILDEP TVGLDQMAIS NLSKMLVAMK QTTRIVIVSH DVDFIFETAD KIIHLHQGKI IHQTTVNDFF SNTSWLMQYG ITPPVIIQAV KMFNEKGIAF KNQAEIKNLD DLISELKNLF SCKKPVF // ID Y307_MYCGE Reviewed; 1177 AA. AC P47549; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=Uncharacterized lipoprotein MG307; DE Flags: Precursor; GN OrderedLocusNames=MG307; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 682-1058. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; L43967; AAC71529.1; -; Genomic_DNA. DR EMBL; U01767; AAD10584.1; -; Genomic_DNA. DR PIR; I64233; I64233. DR RefSeq; WP_010869421.1; NC_000908.2. DR STRING; 243273.MgenG_010200002524; -. DR EnsemblBacteria; AAC71529; AAC71529; MG_307. DR KEGG; mge:MG_307; -. DR PATRIC; 20010144; VBIMycGen98045_0358. DR OMA; WYENNED; -. DR OrthoDB; EOG6TXQRZ; -. DR BioCyc; MGEN243273:GH2R-343-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022186; DUF3713. DR Pfam; PF12506; DUF3713; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 26 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 27 1177 Uncharacterized lipoprotein MG307. FT /FTId=PRO_0000014030. FT LIPID 27 27 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 27 27 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 1177 AA; 131882 MW; 276115B041B75F64 CRC64; MKKLLKKSKF WWFLLCGLSV STILVACSTP TNSALQTVFS PTSTNFFHGQ KGSLKEGLIT ALKTPSANKH FVIGPLLKAL EAWYENNEDK AINKFLKDTK KNVDDQYKNT VNGLISPPRN RAVFIQQDLL DKSGGSEASW KSQQLFNQLI SDFTAKLFAK DFLVYKPNGQ LSTGPYIYDE LSQPEKWKDF GFQEPRFSET NDALFAKLQA QIFNLWVEYT DPTLISQATF KYAAPQQGLG QVYNTEKLKD KLTPSYAFPF FPKDGEIPQN QNVGNKRWEQ LIEGKDGLNT AKTGLEKYIL DQNQGNLIDF PTTLSDNTQT KQIVDSLNIV DQLEAANLGA SLNLKLDLLN QDKDQLPTIK ELNKELNNTI VVESTKIENH TKSNTLFCEH NTTDSSQNNL KSLIKDAFIS SNDSSNLGKL AKQIHQTTTS DMMVSTKASS STTSSYLVWD AAIPNNKTNN GASTVSANCA NATVQNTSHN SNNQLKLRLV RNGEGVAVIG IDGGSYYLTK NSSSKTERDI EKQKQFLMWR AFQAKTNTFK NSLYSFSFPL NETLKTWFEK NQELILVNAL INTDFQKKDK GSDAMQKAFN DYKELMQKFA PVALATNVIR DLFLQMDALD NKLTSRTTEL NTNVNQINPT PWLNGLSSHL PYVRKSGHYE KLNNYFLFLI TKTLWKKVGS EKINISENNN KLKTTKADVD KIRDEILSDI NNKVTEFVNQ LKVTEKSKPN FSNIILVDIN NDQSLTNSAN WSLNALLDVT TVNPLSFALL KNAFTSNQQF EKAKKLFEEI KSKNGSSSTS SSSDADSLAK VISNYYYMTW SKLTNKAMYG NPNNGNIDEL FKKAFLESVD ESGFNVNFKA VIDHYRFIFT LQWLIENNLK NFKDILQANL KYGEIAYIAY DKNIISNNTN NPQGIFGSVF NYENDEHATT ANANQTIDPN NFFFKTKTSP NTTPATTMLS TRQAVSTSNN GTYGFTGLNT TNSSMLENNT NQALLNHIAA NSLKQYGSKD DLKKFISETK DQLVLDNIAR QLSRLTPSSS SSNGKTLSAY FQVDAINNSA LDFKAKQALL LAVLDQYSSY FNSSNSPSIS KRSTQTNQKF SEFNFGGDSY NYLQFTKSDI DSLSLTSSTN IESDIVAALV LFQASDTGTQ QLALSAIEKP QFRIGDKRIQ SGLNLLK // ID Y308_MYCGE Reviewed; 410 AA. AC P52271; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Probable ATP-dependent RNA helicase MG308; DE EC=3.6.4.13; GN OrderedLocusNames=MG308; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71530.1; -; Genomic_DNA. DR EMBL; U02200; AAD12489.1; -; Genomic_DNA. DR PIR; A64234; A64234. DR RefSeq; WP_010869422.1; NC_000908.2. DR ProteinModelPortal; P52271; -. DR STRING; 243273.MgenG_010200002529; -. DR EnsemblBacteria; AAC71530; AAC71530; MG_308. DR KEGG; mge:MG_308; -. DR PATRIC; 20010146; VBIMycGen98045_0359. DR eggNOG; ENOG4105C1J; Bacteria. DR eggNOG; COG0513; LUCA. DR OMA; CAEPAND; -. DR OrthoDB; EOG6GBMBM; -. DR BioCyc; MGEN243273:GH2R-344-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. 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 Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 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; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; RNA-binding. FT CHAIN 1 410 Probable ATP-dependent RNA helicase FT MG308. FT /FTId=PRO_0000055112. FT DOMAIN 26 179 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 190 357 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 39 46 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 126 129 DEID box. SQ SEQUENCE 410 AA; 47990 MW; 953E3751ED3CEED7 CRC64; MQFSSSIRQF LDKKRIVEFT KIQQAVFKLW PFQNIIGIAE TGSGKTFAYL LPLLDKINTS LDQPQAVIFV PTKELQWQII NILTEIKKYF KTFTFATSFS SKAQLIVSLL NEKYLFTSKV RYVVFDEIDM FLEQSSIQQW LECVHLFQKA KPLFAFFSAT LFNQQLQIIK KQVINTKVIN LHPKQWIHPL VKHFVVHLNT ENRFSGLLAL LKHHQNQQII VFCSNQKSLK QLTQLLSNNN ISFGSIYGSL TYQERKNNFT KATNNKLKLL VVSDLFSRGI DLNYFSVVIS WDLPKIDSFY IHRSGRVARL NSWGRSYLFW NDQNQSKLNK LIAKGIKFQN VSLTSNGDLK FLTENNQKTT KKPLSTLQIK KIKAIKAKYK KVKPNYKKYQ KQQIQNLLIN KKKPRSWKNF // ID Y313_MYCGE Reviewed; 287 AA. AC Q49414; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 04-MAY-2001, sequence version 3. DT 13-APR-2016, entry version 69. DE RecName: Full=Uncharacterized protein MG313; GN OrderedLocusNames=MG313; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71535.1; -; Genomic_DNA. DR RefSeq; WP_010869425.1; NC_000908.2. DR STRING; 243273.MgenG_010200003235; -. DR EnsemblBacteria; AAC71535; AAC71535; MG_313. DR KEGG; mge:MG_313; -. DR PATRIC; 20010156; VBIMycGen98045_0364. DR eggNOG; ENOG4106VCR; Bacteria. DR eggNOG; ENOG410YRQW; LUCA. DR OMA; LITIPIY; -. DR OrthoDB; EOG6GTZG2; -. DR BioCyc; MGEN243273:GH2R-349-MONOMER; -. DR Proteomes; UP000000807; Chromosome. 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; Reference proteome. FT CHAIN 1 287 Uncharacterized protein MG313. FT /FTId=PRO_0000210526. SQ SEQUENCE 287 AA; 32963 MW; BB3CFE7B400C966C CRC64; MFPYYPLRLL KSLQLLVWAS VLLALTFIFS IFSISVTNVL SISFLRIPFA LFGWIFGPIW GFIFGFLSDT IDWLTKGYVW FWMFALQKPL FAFLAGIVKG IYLVRKNASN YKVDFWVLQT LLVTFFVVSV TLLLLYLTNN EFQQIGTKNF QTADLSVNVV VLQIITLVSF VIFFLVTEGF LGFVYVKKRN KEQALLTIYS LVLMVLMSVV VSILLGTIAA IEFITFINNG RPSNNFVLYG VYFFLLPRVL VQALLLPIYV ALFYPLIGIV ENNLKNYLLL FTLSWKS // ID Y067_MYCGE Reviewed; 516 AA. AC P47313; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=Uncharacterized lipoprotein MG067; DE Flags: Precursor; GN OrderedLocusNames=MG067; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; L43967; AAC71285.1; -; Genomic_DNA. DR PIR; D64207; D64207. DR STRING; 243273.MgenG_010200001265; -. DR EnsemblBacteria; AAC71285; AAC71285; MG_067. DR KEGG; mge:MG_067; -. DR PATRIC; 20009520; VBIMycGen98045_0069. DR OMA; QEWIRPA; -. DR OrthoDB; EOG61S2V3; -. DR BioCyc; MGEN243273:GH2R-70-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022382; DUF31. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 516 Uncharacterized lipoprotein MG067. FT /FTId=PRO_0000018735. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 516 AA; 59063 MW; B6B591A25D667288 CRC64; MLYRFWKTGL AIFMPGCILL SSCSFRSYIP TPSLRNTVGN HNSYVNNTVP KNNFYEKFYD LTFALNFTNQ KTQEFGTGWL IDWKGDETKD LNTLTIASSS IISSVSNHSL KEKQDDKLFI AYIATNLHLI DGLKNDHDYQ PYNKDGNGLS FPFDQKTQSF LLGRFANPKI NSKPEEMNYQ VQTRLKQDAM VFIQTSTLPK TAYAGIDPIN FDYHETSDES GFWTKKQSTA NFPRTRTLKS YADFAVLEVP LFLDNANDAK IYQEWIRPAV QAYKELGDVE NIFAKTPYAE YINNTYYLLG YPVTNNNKYQ FILGQDEKWK FSQQTSVLKH YQKQPLQQRT VYVERDDGLP TLTFNEDKLT HVQGTDLINV DQITDTNLGN GLINYAGLSR FTLSYHNVEY KLFGYGTILN NTNFPGGSSG SAVFNKEKQL TSIYFGSLIN VTTGNNRNVN LGLGQILRTY NTNNSKHSAP SSYDLIFGDK NTIKFYAQFA KEKQTHLWNK IQTSVNSSIS FYKDKK // ID Y076_MYCGE Reviewed; 138 AA. AC P47322; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 73. DE RecName: Full=Uncharacterized protein MG076; GN OrderedLocusNames=MG076; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71294.1; -; Genomic_DNA. DR PIR; D64208; D64208. DR RefSeq; WP_009885931.1; NZ_AAGX01000011.1. DR STRING; 243273.MgenG_010200002881; -. DR EnsemblBacteria; AAC71294; AAC71294; MG_076. DR KEGG; mge:MG_076; -. DR PATRIC; 20009554; VBIMycGen98045_0086. DR OMA; RYEISKF; -. DR OrthoDB; EOG654PCW; -. DR BioCyc; MGEN243273:GH2R-79-MONOMER; -. DR Proteomes; UP000000807; 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 1 138 Uncharacterized protein MG076. FT /FTId=PRO_0000210413. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. SQ SEQUENCE 138 AA; 15867 MW; 204E568264CCB8C0 CRC64; MVLNQNKNSN KAEYGGIVVS VFYLILFFLI LNITIYFHKS TNFTVVVKNS VLTSFFVNLL LVCLQGIFRL KTCDGMRYEI SKFNRYLKLG SVYAKPLVSF NQYQDQSATY RQKTSGFWWM NLIVYLVGSL VSGLVSLL // ID Y120_MYCGE Reviewed; 520 AA. AC P47366; Q49272; Q49275; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Uncharacterized protein MG120; GN OrderedLocusNames=MG120; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-86 AND 446-520. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71338.1; -; Genomic_DNA. DR EMBL; U02147; AAD12427.1; -; Genomic_DNA. DR EMBL; U02143; AAD12422.1; -; Genomic_DNA. DR PIR; C64213; C64213. DR RefSeq; WP_010869341.1; NZ_AAGX01000002.1. DR STRING; 243273.MgenG_010200000855; -. DR EnsemblBacteria; AAC71338; AAC71338; MG_120. DR KEGG; mge:MG_120; -. DR PATRIC; 20009644; VBIMycGen98045_0131. DR eggNOG; ENOG41083U2; Bacteria. DR eggNOG; COG4603; LUCA. DR KO; K02057; -. DR OMA; SQFERIN; -. DR OrthoDB; EOG6MSS3R; -. DR BioCyc; MGEN243273:GH2R-124-MONOMER; -. DR Proteomes; UP000000807; 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:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 520 Uncharacterized protein MG120. FT /FTId=PRO_0000210423. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT TRANSMEM 138 158 Helical. {ECO:0000255}. FT TRANSMEM 167 187 Helical. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TRANSMEM 271 291 Helical. {ECO:0000255}. FT TRANSMEM 318 338 Helical. {ECO:0000255}. FT TRANSMEM 355 375 Helical. {ECO:0000255}. FT CONFLICT 12 15 HHLV -> TPPG (in Ref. 2; AAD12427). FT {ECO:0000305}. FT CONFLICT 79 86 NFLRQIAI -> KFLKTDCY (in Ref. 2; FT AAD12427). {ECO:0000305}. FT CONFLICT 446 453 QEYHHNCA -> EYHQQIVQ (in Ref. 2). FT {ECO:0000305}. FT CONFLICT 499 499 S -> I (in Ref. 2; AAD12422). FT {ECO:0000305}. SQ SEQUENCE 520 AA; 58840 MW; D0E8E7FDA1F06A3E CRC64; MTMWQFKSYF KHHLVFWKDR FLHSSEKQMQ RRSILSSVVL IILSFLISFL LIISIPGGRG ASFFALFTKL FLDNTNTENF LRQIAIYILA GLAFSFCMSV GIFNIGISGQ MMAGAIFGFL MILKVFPSSF RPGFGGQIIT VLLMVIGSVS VAVVVATLKI FFKVNEVVSA IMLNWIVVLI SAYLVETYIK DNSGGTAQFF SLPLPDEFAL YNFSPLTKKF GWLASLIIAF ISVIIVAVVL KYTVFGHKLK SIGSSVFGSQ AMGFNVRKYQ FLSFIISGIL SGLLATVVYT ASTEKVLTFN NVGDSAISAV PATGFDGIAI GLIALNNPFR IVIVSVLIAF VNIGARPANL NPNTASLVLG IMMYFAALYN LMVYFKPWRY LVKLNIGKIN LTTYETYENK LAANLEWLSF QRFLSKQKKK NDKTKFNWFD TSLFEQYAKN KQEIVQEYHH NCATNLIAWW LNAIQSGNIK PSTTFKLEFV NFKHQQKFVL NWFKNESESL RDFQSQFERI NKLVEREFVK // ID Y185_MYCGE Reviewed; 701 AA. AC P47431; Q49380; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Uncharacterized lipoprotein MG185; DE Flags: Precursor; GN OrderedLocusNames=MG185; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 525-701. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8524858; DOI=10.1073/pnas.92.25.11829; RA Peterson S.N., Bailey C.C., Jensen J.S., Borre M.B., King E.S., RA Bott K.F., Hutchison C.A. III; RT "Characterization of repetitive DNA in the Mycoplasma genitalium RT genome: possible role in the generation of antigenic variation."; RL Proc. Natl. Acad. Sci. U.S.A. 92:11829-11833(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; L43967; AAC71404.1; -; Genomic_DNA. DR EMBL; U34967; AAA88885.1; -; Genomic_DNA. DR PIR; E64220; E64220. DR RefSeq; WP_009885871.1; NZ_AAGX01000007.1. DR STRING; 243273.MgenG_010200002344; -. DR EnsemblBacteria; AAC71404; AAC71404; MG_185. DR KEGG; mge:MG_185; -. DR PATRIC; 20009804; VBIMycGen98045_0208. DR eggNOG; ENOG4106J71; Bacteria. DR eggNOG; ENOG410Y9FZ; LUCA. DR OMA; NEDELMI; -. DR OrthoDB; EOG6JMMQZ; -. DR BioCyc; MGEN243273:GH2R-194-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004890; Lipoprotein_10_C. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03202; Lipoprotein_10; 1. DR Pfam; PF03305; Lipoprotein_X; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 701 Uncharacterized lipoprotein MG185. FT /FTId=PRO_0000018723. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CONFLICT 525 528 GKTA -> WQNC (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 701 AA; 77634 MW; 5E0E2A821ED5C006 CRC64; MKFKLFFLSS SVLGPIALFT TACSAVYRFD QVDDGKIKLA TVTSASASGS LTTIISKYNS QKDPNDYPVE LVSLDSRGSY SNGKKDLQAK LLAKDKNNFY NLTFNYSDVV SILSRSQMEL SFDTVDTSNF DPSFLSFNNN ISNVNPNSIY ALPATVSGEV LVLNGPVLHY ILSSAKKDSN TTLSTHSASN NSNKGTMVVA SDSETSSLWT KLEAAAKMNA QTNETQVLKS NSSESNQTQA SDTEIKKIWG DYQEVDGGLK NYTFKASVFN NWKDLNDFAT RIAKSFTKLQ TTTKKGEEVQ AVFGIGSLEN ALYTALFASG KADYNNFLFN IKNQRINFSN FFNKSSTAFQ NLKTIFNSFK SLIDQNGLIS NAHFNTPVND YAKFNQLAFY TSSTARFPYS FASDSVKRLI VNDKTIENKN NKSVFEVNLS SDSDNNSNLI GTVSLENSKQ VSLYEKQVDS NKQIGVDALL IKDETLINHL KSLKSQVSAK SASETSQTKQ NKTFLAFTTV NADQKAIFDV GKLNGKTAKI IINATETTNA KISTLQEKEA IVLKAPQRFE STDPFPIALV QGPSLIGIHA NEREDIETKK FVNWYLNTKV QWEENSIKTP AEYVADKASY LLPFKNRLNN TNSYNEFVKT AVSQFADKNV TKFAEPADFL SNKVRDGVKS NLNAAINNHS IDFDSFINDL TDYLGSDVKN I // ID Y186_MYCGE Reviewed; 250 AA. AC P47432; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 92. DE RecName: Full=Uncharacterized lipoprotein MG186; DE Flags: Precursor; GN OrderedLocusNames=MG186; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Contains 1 TNase-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00272}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71405.1; -; Genomic_DNA. DR PIR; F64220; F64220. DR RefSeq; WP_010869364.1; NC_000908.2. DR ProteinModelPortal; P47432; -. DR STRING; 243273.MgenG_010200003373; -. DR EnsemblBacteria; AAC71405; AAC71405; MG_186. DR KEGG; mge:MG_186; -. DR PATRIC; 20009812; VBIMycGen98045_0212. DR eggNOG; COG1525; LUCA. DR KO; K02027; -. DR OMA; NAKINIW; -. DR OrthoDB; EOG6HF5WJ; -. DR BioCyc; MGEN243273:GH2R-195-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 2.40.50.90; -; 1. DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold. DR InterPro; IPR002071; Thermonucl_AS. DR SMART; SM00318; SNc; 1. DR SUPFAM; SSF50199; SSF50199; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS01123; TNASE_1; 1. DR PROSITE; PS50830; TNASE_3; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Endonuclease; Hydrolase; KW Lipoprotein; Membrane; Nuclease; Palmitate; Reference proteome; KW Signal. FT SIGNAL 1 24 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 25 250 Uncharacterized lipoprotein MG186. FT /FTId=PRO_0000034398. FT DOMAIN 44 200 TNase-like. {ECO:0000255|PROSITE- FT ProRule:PRU00272}. FT LIPID 25 25 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 25 25 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 250 AA; 28288 MW; E3C00A92D99650D9 CRC64; MKGFLKPNFS LGALFLTLSP IATACIAEKP VNNRFNFNSE QLARLRKARV NHWRDGDTLE VSFANNHQKP IRIYAIDTPE KAVLSIQRKS EIELKEANKA TEFAKSLIPI GSEVWIWPLN SYSYDREVAA VFFKTNPLQL HFESFAVEMV ANGHALPIAG NDFDFVFSDL DPFNPLKIVG IELANGLNNA FNNRKNIFSY LENSFQSITM VYQQRGVDQS WTRYLAPSND FSSTKLGLGL TIYELKLNNG // ID Y199_MYCGE Reviewed; 167 AA. AC P47441; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 58. DE RecName: Full=Uncharacterized protein MG199; GN OrderedLocusNames=MG199; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; I64221; I64221. DR ProteinModelPortal; P47441; -. DR STRING; 243273.MgenG_010200001327; -. DR eggNOG; ENOG4107FSS; Bacteria. DR eggNOG; COG1039; LUCA. DR OMA; ARDSFIN; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. 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 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 167 Uncharacterized protein MG199. FT /FTId=PRO_0000210450. SQ SEQUENCE 167 AA; 19311 MW; 427AA5C2D80B7D96 CRC64; MDHHTITLDP KQYNDLTKSL KNTNLLLTNL HCQLYQKLLE KNQLLRQTVT ISIDQFANQE LFVNYLNKLT NFTDKTVLLP DQFLINGETK SLVIAAASIL ARDSFINQLQ LLNQKVNYDL PKGSSHGIEQ ALLFLNQQRG FSQIEQFKQV AKLNFKNVTK FLQQLVY // ID Y209_MYCGE Reviewed; 308 AA. AC P47451; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Uncharacterized RNA pseudouridine synthase MG209; DE EC=5.4.99.-; DE AltName: Full=RNA pseudouridylate synthase; DE AltName: Full=RNA-uridine isomerase; GN OrderedLocusNames=MG209; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-243. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: RNA uridine = RNA pseudouridine. CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00182}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71427.1; -; Genomic_DNA. DR EMBL; U02214; AAD12509.1; -; Genomic_DNA. DR PIR; A64223; A64223. DR RefSeq; WP_009885746.1; NZ_AAGX01000004.1. DR ProteinModelPortal; P47451; -. DR STRING; 243273.MgenG_010200001397; -. DR EnsemblBacteria; AAC71427; AAC71427; MG_209. DR KEGG; mge:MG_209; -. DR PATRIC; 20009872; VBIMycGen98045_0241. DR eggNOG; ENOG4105C34; Bacteria. DR eggNOG; COG0564; LUCA. DR KO; K06180; -. DR OMA; EIDCGIN; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; MGEN243273:GH2R-218-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. 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; Isomerase; Reference proteome; RNA-binding. FT CHAIN 1 308 Uncharacterized RNA pseudouridine FT synthase MG209. FT /FTId=PRO_0000162739. FT DOMAIN 11 87 S4 RNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00182}. FT ACT_SITE 131 131 {ECO:0000250}. SQ SEQUENCE 308 AA; 34996 MW; F2850BAD06A125A2 CRC64; MKQCFVVTTT KRLDSLLASL LNLSRVKVVK LIMNGQIKVN EKLTFKNSLI VAKDDVIKVE IHDETTSDFI TSVEPYNLKL EVLFEDKDLM VINKPSGLLT HPTTFNEKAS LLAACIFHNN KNPVYLVHRL DRDTSGAIVV CKNQASLLNL QNQLQNRTLK RYYVALVHFP FNALTGSINA PLARVNNNKV MFKIAQTAKA KQAITKFKVI NQNEKAALIS LELLTGRTHQ IRVHLKFIQH PVYNDPLYGI KSEKKDSYGQ FLHANRICFI HPTLNKPMDF HAPLEPKFST KLKSLNLSLT DPLHVLFK // ID Y223_MYCGE Reviewed; 411 AA. AC P47465; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 60. DE RecName: Full=Uncharacterized protein MG223; GN OrderedLocusNames=MG223; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71444.1; -; Genomic_DNA. DR PIR; F64224; F64224. DR RefSeq; WP_010869381.1; NZ_AAGX01000004.1. DR STRING; 243273.MgenG_010200001497; -. DR EnsemblBacteria; AAC71444; AAC71444; MG_223. DR KEGG; mge:MG_223; -. DR PATRIC; 20009926; VBIMycGen98045_0259. DR OMA; FMDNALV; -. DR OrthoDB; EOG65QWFP; -. DR BioCyc; MGEN243273:GH2R-245-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 411 Uncharacterized protein MG223. FT /FTId=PRO_0000210465. SQ SEQUENCE 411 AA; 47824 MW; 91CCD0DFDBAA0ED9 CRC64; MYKPKNINSV LTFYKDQIQL VVSDDQNQFN ILFYQTIDND GFYSKQQLKN KLRLKLALNQ LVDQANYFLG FKLEKVVVVL AELIDDLKIH NFKSEIFFTG YDFDHKAMIK KEKQRFCEQN NQLTVMDTMV LNYHDVINNK ITKSFAFNKS YVANLVAYSS KSNLIGELKF FLKRNVNLKV KKIISHHLAL ANSLSKKQNN MFVYLGQKTT ELMLFMDNAL VDVITNQFGK NHFIDIPANQ ENKPLLEFLV DNTTKIGDCY SLGMTYTDGD SYKEIKALTI GDLMQTVSDK IKTLIDFINS GSLTFFNKFK TLPKLLYFYT RSKQITNLFQ ANVALINPQF KTVDIYKNKI QFISENYLLS CEAISLQITN RIKNQISFDF TNADNIQKPK PKKHFMILSK HLTKFVQRLV K // ID Y226_MYCGE Reviewed; 459 AA. AC P47468; Q49367; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Uncharacterized protein MG226; GN OrderedLocusNames=MG226; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.genitalium MG225. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD12530.1; 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; L43967; AAC71447.1; -; Genomic_DNA. DR EMBL; U02264; AAD12530.1; ALT_INIT; Genomic_DNA. DR PIR; I64224; I64224. DR TCDB; 2.A.3.6.5; the amino acid-polyamine-organocation (apc) family. DR EnsemblBacteria; AAC71447; AAC71447; MG_226. DR KEGG; mge:MG_226; -. DR PATRIC; 20009932; VBIMycGen98045_0262. DR OMA; FFQGWNQ; -. DR OrthoDB; EOG6F55D5; -. DR BioCyc; MGEN243273:GH2R-248-MONOMER; -. DR Proteomes; UP000000807; 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:0015171; F:amino acid transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002293; AA/rel_permease1. DR Pfam; PF13520; AA_permease_2; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 459 Uncharacterized protein MG226. FT /FTId=PRO_0000210469. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 74 94 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 129 149 Helical. {ECO:0000255}. FT TRANSMEM 177 197 Helical. {ECO:0000255}. FT TRANSMEM 210 230 Helical. {ECO:0000255}. FT TRANSMEM 258 278 Helical. {ECO:0000255}. FT TRANSMEM 317 337 Helical. {ECO:0000255}. FT TRANSMEM 361 381 Helical. {ECO:0000255}. FT TRANSMEM 396 416 Helical. {ECO:0000255}. FT TRANSMEM 421 441 Helical. {ECO:0000255}. SQ SEQUENCE 459 AA; 50695 MW; F086ECA5A552A928 CRC64; MTMFDVGPFS YLVLGLTSFA ILGVVLSFSR LSVLCGNSAY GGSYLIAKKA VGTNSKTKRF FVFLSGWNVS LTGSFNGVVI PAVLIFSFAD IPVVKANNNI IIGLLVGGFL LFGLLTFISL FGLKINKKAI FYFAVIKWIV VIGGFILGIY LIGTTNGKGF VENNLIGTRE NIDFFKIIFI SLALTIAFAG TEDLASITPD VKSNNLRKCF LIAFGCVVLL YLVGFVIISG LDGIRGYGLA LGNKDPKAIN NYGSIYRLVG GVPLLVIYGL GLLVNSLASR LSMTITTARK YVALAQDGFL PSFLAKTNKH NEYHHAVLIS NLMTLLVMLI MVIIPFLPDH NNNNNSLFNA IEQLVTVTIE MAAAISLIQY FITFIFFFMI FAKKENQKLI PLWEKVSYVI SFALVSVLLF VPLFPFNQWT VFNTFKIVVL ICFYLLGVGF FGYAEWKNKN KYQLMNNNS // ID Y240_MYCGE Reviewed; 292 AA. AC P47482; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Uncharacterized protein MG240; GN OrderedLocusNames=MG240; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-292. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Contains 1 HD 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; L43967; AAC71461.1; -; Genomic_DNA. DR EMBL; U01734; AAD10544.1; -; Genomic_DNA. DR PIR; E64226; E64226. DR ProteinModelPortal; P47482; -. DR STRING; 243273.MgenG_010200001627; -. DR EnsemblBacteria; AAC71461; AAC71461; MG_240. DR KEGG; mge:MG_240; -. DR PATRIC; 20009962; VBIMycGen98045_0277. DR eggNOG; ENOG4108H0C; Bacteria. DR eggNOG; COG1057; LUCA. DR eggNOG; COG1713; LUCA. DR KO; K00969; -. DR OMA; NAFSINT; -. DR OrthoDB; EOG6F55KJ; -. DR BioCyc; MGEN243273:GH2R-262-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.3210.10; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR005249; CHP00488. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00488; TIGR00488; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 292 Uncharacterized protein MG240. FT /FTId=PRO_0000210477. FT DOMAIN 140 252 HD. SQ SEQUENCE 292 AA; 33551 MW; 9A8518BD0FAD54DC CRC64; MLKLAIKSVN NALVSNFDIK TKNAFSINTV NHFKSCYPTS EIYFLIGSDK LNELEKWDHI QQLKDLCTFV CYERKPYPFN KKIANQFNVK YLAKCPLEIA SSKLLNQPRK KLIPLAVLNY INTNHLYLIP TLKAMVDDKR FQHCLRVGKL AKQLAIANKL DAKRAFVAGA YHDLAKQLPV DQLVNIATSE LKITNYPSWK VLHSYVGAYI LKNWFGVKDK MIINAIKNHT IPPKQVSKLD MIVYLADKLE PNRKQEQWSG GIEIDQLVKL AKSNLKQAYL ITLKYVQNLV KD // ID Y246_MYCGE Reviewed; 281 AA. AC P47488; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=Uncharacterized protein MG246; GN OrderedLocusNames=MG246; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71466.1; -; Genomic_DNA. DR PIR; B64227; B64227. DR RefSeq; WP_010869391.1; NC_000908.2. DR ProteinModelPortal; P47488; -. DR SMR; P47488; 1-280. DR STRING; 243273.MgenG_010200001687; -. DR EnsemblBacteria; AAC71466; AAC71466; MG_246. DR KEGG; mge:MG_246; -. DR PATRIC; 20009974; VBIMycGen98045_0283. DR eggNOG; ENOG4105D48; Bacteria. DR eggNOG; COG1692; LUCA. DR KO; K09769; -. DR OMA; PTADAQI; -. DR OrthoDB; EOG68DD2S; -. DR BioCyc; MGEN243273:GH2R-268-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR005235; YmdB-like. DR Pfam; PF13277; YmdB; 1. DR PIRSF; PIRSF004789; DR1281; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00282; TIGR00282; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 281 Uncharacterized protein MG246. FT /FTId=PRO_0000210485. SQ SEQUENCE 281 AA; 31595 MW; 7BC4A993A879ED22 CRC64; MDNIKVLFLG DVYGKAGRKI ISDHLPIIKK KYQLNLIIAN AENTTNGKGL SWNHYQILKQ AGIDYITMGN HTWFQKQDLE LVLNQVDVIR PLNLMQDFNY FQLGKGSYLF SLNGLKIRIT NLLGTSINLP FAITNPFVEL KKLVLTKDCD LHIVDFHAET TSEKNAFCMV FDGYVTAILG THTHVPSNDL RITPKGSVYI TDVGMCGPGF GSVIGANPKQ SIKLFCTGER QFFEVSNCGA QLNGVFFEVC SKTNQVVKIE QIRIVLDDEK YLANDYFNLV E // ID Y302_MYCGE Reviewed; 317 AA. AC P47544; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Uncharacterized protein MG302; GN OrderedLocusNames=MG302; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CbiQ 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; L43967; AAC71524.1; -; Genomic_DNA. DR PIR; D64233; D64233. DR RefSeq; WP_010869418.1; NC_000908.2. DR EnsemblBacteria; AAC71524; AAC71524; MG_302. DR KEGG; mge:MG_302; -. DR PATRIC; 20010134; VBIMycGen98045_0353. DR KO; K16785; -. DR OrthoDB; EOG66MQPD; -. DR BioCyc; MGEN243273:GH2R-338-MONOMER; -. DR Proteomes; UP000000807; 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; IPR003339; ABC/ECF_trnsptr_transmembrane. DR Pfam; PF02361; CbiQ; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 317 Uncharacterized protein MG302. FT /FTId=PRO_0000210522. FT TRANSMEM 18 38 Helical. {ECO:0000255}. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TRANSMEM 130 150 Helical. {ECO:0000255}. FT TRANSMEM 159 179 Helical. {ECO:0000255}. FT TRANSMEM 202 222 Helical. {ECO:0000255}. FT TRANSMEM 252 272 Helical. {ECO:0000255}. SQ SEQUENCE 317 AA; 36668 MW; BC697418D52836B0 CRC64; MQKTSFLNKI DPLLKLWFWL ISLVVAFLPL GLYGLVIINL VFLTLVVISE KRVKSALIIL SWMLFFLWFN VIVNGFIFLP NTALSVDQNH NFLGSFIYSG GNNFGGVSWW SFNLRSFLRS FVIALRISML FSASFLLTTS SSIYELAWAV ERFFKFLKLF HIKVQPISIL LAVIFKLLPT VKSEIIRIKQ AQATRGFIYN KCSFLNPFKI KTLFIPVLLS TVKKTETTAF ALQAKGYDLN NTNRTHYPLK YNLLNGVFLL VGLLLFSILL IANNWNLVYW ENPNYSFNFD KQNFIFLRAI NSNNLLYFWQ IELIAIG // ID Y326_MYCGE Reviewed; 295 AA. AC P47568; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=DegV domain-containing protein MG326; GN OrderedLocusNames=MG326; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71550.1; -; Genomic_DNA. DR PIR; A64236; A64236. DR RefSeq; WP_009885962.1; NZ_AAGX01000013.1. DR ProteinModelPortal; P47568; -. DR STRING; 243273.MgenG_010200003068; -. DR EnsemblBacteria; AAC71550; AAC71550; MG_326. DR KEGG; mge:MG_326; -. DR PATRIC; 20010208; VBIMycGen98045_0381. DR eggNOG; ENOG4108589; Bacteria. DR eggNOG; COG1307; LUCA. DR OMA; PEKGETW; -. DR OrthoDB; EOG6HB9NH; -. DR BioCyc; MGEN243273:GH2R-374-MONOMER; -. DR Proteomes; UP000000807; 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 1 295 DegV domain-containing protein MG326. FT /FTId=PRO_0000209772. FT DOMAIN 4 292 DegV. {ECO:0000255|PROSITE- FT ProRule:PRU00815}. FT BINDING 63 63 Fatty acid. {ECO:0000250}. FT BINDING 95 95 Fatty acid. {ECO:0000250}. SQ SEQUENCE 295 AA; 33413 MW; 04610881C0F841EE CRC64; MKKTAIITDS TASIKPGEIN GVYILPLQVI VDGEKSFRDG IEIDYDHVHK LLKENPHGLN ISTSLPRQSD LLKIFEEIKT KYDRFIFLPL SKGLSGTYDM LVQLAKELSE QNKDKEFLVF ETSDIAISLK WLVEDIKALV DKGCDNQTIK AKVESHKQNI LSAVTLKNLV QMRKGGRISG LKKFITTLLR VKPIILFDKG VNTLGAKVFS FSQAVEKIFG FVKTKFGDNY KIKRIGFCYS FCKNYANEIK KIITDFIEHN KINFQNEIEN AFITSVIIVH TGIDAFSISL LIDNK // ID Y337_MYCGE Reviewed; 138 AA. AC P47579; Q49514; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 62. DE RecName: Full=Uncharacterized protein MG337; GN OrderedLocusNames=MG337; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-138. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71562.1; -; Genomic_DNA. DR EMBL; U01709; AAB01021.1; -; Genomic_DNA. DR PIR; C64237; C64237. DR RefSeq; WP_009885968.1; NZ_AAGX01000014.1. DR ProteinModelPortal; P47579; -. DR STRING; 243273.MgenG_010200003126; -. DR EnsemblBacteria; AAC71562; AAC71562; MG_337. DR KEGG; mge:MG_337; -. DR PATRIC; 20010234; VBIMycGen98045_0394. DR eggNOG; COG0822; LUCA. DR OMA; MDIRART; -. DR OrthoDB; EOG6GFGQT; -. DR BioCyc; MGEN243273:GH2R-387-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N. DR Pfam; PF01592; NifU_N; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 138 Uncharacterized protein MG337. FT /FTId=PRO_0000210547. FT CONFLICT 52 56 ITAIG -> NYCNW (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 138 AA; 15720 MW; D993716EC6298CE8 CRC64; MDIRARTKII DIYSNLKYKK PLKSFQKILT TSDSDNCEDF FNIGLNIDKN KITAIGFDGD GCIISTIATE LSIKAIENKT INQAKKILSD LIATYKDKNS ANQVVEELKL LIEMNVTEKR LQCLLLTPSN LLQWFKNF // ID Y373_MYCGE Reviewed; 281 AA. AC P47613; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 68. DE RecName: Full=Uncharacterized protein MG373; GN OrderedLocusNames=MG373; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71600.1; -; Genomic_DNA. DR PIR; C64241; C64241. DR RefSeq; WP_009885938.1; NZ_AAGX01000012.1. DR STRING; 243273.MgenG_010200002916; -. DR EnsemblBacteria; AAC71600; AAC71600; MG_373. DR KEGG; mge:MG_373; -. DR PATRIC; 20010328; VBIMycGen98045_0438. DR eggNOG; ENOG41060PX; Bacteria. DR eggNOG; ENOG41125D5; LUCA. DR OMA; RICLTYQ; -. DR OrthoDB; EOG6QP0XX; -. DR BioCyc; MGEN243273:GH2R-428-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR Gene3D; 3.90.320.10; -; 2. DR InterPro; IPR011604; Exonuc_phg/RecB_C. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR019080; YqaJ_viral_recombinase. DR Pfam; PF09588; YqaJ; 1. DR SUPFAM; SSF52980; SSF52980; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 281 Uncharacterized protein MG373. FT /FTId=PRO_0000210574. SQ SEQUENCE 281 AA; 32521 MW; 17F98BA87FE8A39B CRC64; MGFIKQYKTD FDIVDNQIVL SEQYFLRNKA LFKKITGTRF GKVLGLSEYE SSFKTWANMV KIYEDEFDET LAKAGNIIEP KIRDYVNLKT GFNFHSYDPK KVQFDLFKDD SVFGGIPDGE PLDENGELAY QNDLPMLEIK TTSCDSLIYK KINGNLKMIL DENGMPIVKK KDGKKDSWFD SNGKIIISTL YYCQIGLYLY LRNVNKGLFA IAFLKPEDYV LPEQFNASNR EIRLIPIKID HKGFSVLVDK ARIWYENYIL TGKSPKLTES DIQWLKENGI E // ID Y422_MYCGE Reviewed; 835 AA. AC P47661; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 62. DE RecName: Full=Uncharacterized protein MG422; GN OrderedLocusNames=MG422; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 701-758. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71646.1; -; Genomic_DNA. DR EMBL; U02117; AAD12391.1; -; Genomic_DNA. DR PIR; F64246; F64246. DR RefSeq; WP_010869478.1; NC_000908.2. DR EnsemblBacteria; AAC71646; AAC71646; MG_422. DR KEGG; mge:MG_422; -. DR PATRIC; 20010430; VBIMycGen98045_0488. DR OMA; WFLGFNA; -. DR OrthoDB; EOG6MM1S3; -. DR BioCyc; MGEN243273:GH2R-476-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 835 Uncharacterized protein MG422. FT /FTId=PRO_0000210602. SQ SEQUENCE 835 AA; 99966 MW; 5DBD9A833FF4442E CRC64; MLKKISLFDN LEQWVDLSLL MIRTSFLDAN YFGVAKLSLF KYGNYLIDNL NQAQWKTLSQ VLQLNKQPYS GFLLVNNHQY LPLQKIKFNL CEEIDLRNKN KWLFPNSFSI FLKQDLSYKK DQNYFNLVNI PKQLKWFLGF NALNDLFRFS ILKIENVNQK TSKVINQFFT SKFINSIYFE QVDFEYNNFL TLIEKNEREL VDFNCMFFNQ LFTFNNKVIK SFFERYYALN EQKNNLKNKL KIAAYEAKSR DNSYFEKLQI ERAKQRLFDA KKTFSKQHKN ALQLINSFTF SLIFSGWKIK WRSFFNFYRK RILEKKIVSK RIKTRILLLK EIKKMDLLSP KLLVETIDES INLVNKIFAN IQNLYQEIIS LKSGPNLNWK YQTINQELKI MSARFILTKK EVHEFLIKAR LSFIKNFVKQ SNNLYVHEKL VNELKENILL NQNHYRGKHN NSFSVLIQKT VFKQFIDTVQ YAIGLISMRK SLETFNFAFQ IKQYFYESLL ANYQKINWQK YELNNLYFVL ISLWNSLSKK FQQFFNKYEF LSCGSNDFIW NEGRSEPHFS LLKDKLKNDL NSPKWNFLVD KVINKYLDLN FETPVSFLLA SRGFSSTTDT TNKETKNDLK QKLKKCKQKY KLLLKDINLV KWIFRDETNQ KLQKIKFIMK RYCILNKTLH LRLKKTNKKI KRTFFIDSEE CNINRLEASN KLYLNVLNSQ LKTINFFLRS QKNLKKLNFI NNINLLINQT KKNGISSWML FSDLNKINKN ESLKLYLLFK LLLNPKLLMI NCCNDFTNHA YNFIRGLLIS YQNKQGIALI FNDPNNKLVK NFSIKNIDFE TGMKK // ID Y095_MYCGE Reviewed; 398 AA. AC P47341; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 74. DE RecName: Full=Uncharacterized lipoprotein MG095; DE Flags: Precursor; GN OrderedLocusNames=MG095; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71313.1; -; Genomic_DNA. DR PIR; E64210; E64210. DR RefSeq; WP_009885652.1; NZ_AAGX01000002.1. DR STRING; 243273.MgenG_010200000705; -. DR EnsemblBacteria; AAC71313; AAC71313; MG_095. DR KEGG; mge:MG_095; -. DR PATRIC; 20009592; VBIMycGen98045_0105. DR OMA; GNNNFWF; -. DR OrthoDB; EOG6W720M; -. DR BioCyc; MGEN243273:GH2R-98-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 398 Uncharacterized lipoprotein MG095. FT /FTId=PRO_0000014026. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 398 AA; 44932 MW; 27EF30901AE78F07 CRC64; MKLKFYKLPL ITTAFSFVFL TACSTPQSSF FLPAQTTIST LKINGMENKT GYFLETQRSR GSYNPTASLT MIKLGDEKEF KNVDTTKQDE VLFANIYGGI SSLLNFRIIQ PMLTYWNLVN NSLSQIGSTN DLITFKDSGY KDQLAKALAN NLIVADEGNN NFWFGLKALK FDTVKLQANN TATSSTRAST TQNTNNKIDA REKITINGNG GTNNDQNATV QKLIGIENIE VEFSFVKTGF NGNEIKFEDY VTDSSPTTSL LKQVWKSKWN TELTHTSFKF KLNSFNVLLT YQLEANQKSQ YLPNGFSFLF PSNLEGKIDS SKSYWNNLVD FSKRTTNEEN TMLLTDLQKK QDQVNRFVGF IGQNHFTLSA NSINEKQFND ASTADFFKAI FQKVSINE // ID Y096_MYCGE Reviewed; 650 AA. AC P47342; Q49188; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 71. DE RecName: Full=Uncharacterized protein MG096; GN OrderedLocusNames=MG096; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; L43967; AAC71314.1; -; Genomic_DNA. DR EMBL; U01713; AAC43186.1; -; Unassigned_DNA. DR EMBL; U01762; AAD10577.1; -; Genomic_DNA. DR RefSeq; WP_010869330.1; NC_000908.2. DR STRING; 243273.MgenG_010200000710; -. DR EnsemblBacteria; AAC71314; AAC71314; MG_096. DR KEGG; mge:MG_096; -. DR PATRIC; 20009594; VBIMycGen98045_0106. DR OMA; WSGEMNL; -. DR OrthoDB; EOG6RVG4C; -. DR BioCyc; MGEN243273:GH2R-99-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 650 Uncharacterized protein MG096. FT /FTId=PRO_0000215245. SQ SEQUENCE 650 AA; 74803 MW; 30539DDC6F69DDC3 CRC64; MKTQKNIFKV KALLLSLFSA AVTITIFALP IFANNGSKTD LGLLSKNSAD FLGSSKRSLA GFDTPFSPDN LQYLEKETDY DQNFKSFTEK FKDEKITNNQ LGIVDIYNLF SGFHKSVKST VDLMNQLQKQ VEAANAIFPV DDAFVKLPKV PTELFKLVDD NVFPKLNPKG LNISDNIAAL FERYNLKSIE LKNFDLAFLR KADVIIKDKV RYNFEMQMQF QTVYVGGGNT VINLDFTLKA QTVNFANLQD LQNTFVKVGN DLSTQLFWIP TVNKLTDNAG NDLTHIAKTV IGESFFQTNV NLAKSVIEYD KVQPLVKQAF EERVLTPFKK EREAAKKAYE EEQRRLEEER KRQLEELRRR EAEEKRKAEE AKRNQEKARR EREAYEKSFN SFKDFKFYWL TKGKDVTKKA DLIDALKTAI ATPAYRNRTF SLLIKGFASG VERYFNANKN DKELKKLAFG EKGIQFPRAD AGVNGLYMSN FLRHELTSKA KFSLNLKDIK VENTVEDTQL YWKDNGIHLK QANPYKFNLN IKIKYNGWYN VHWWNWLPAK ILGIPTDWSG EMNLTFVVNG DLSEIVDKHD YPGTFFQFTD KNELLFTLAV REQIKVDNNH FMGLLKSQNL HNLQLASGAT KPPVVDLASY FHFVLLTEKS // ID Y101_MYCGE Reviewed; 222 AA. AC P47347; Q49244; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MG101; GN OrderedLocusNames=MG101; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-132. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Contains 1 HTH gntR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00307}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71319.1; -; Genomic_DNA. DR EMBL; U02103; AAD12375.1; -; Genomic_DNA. DR PIR; B64211; B64211. DR RefSeq; WP_009885659.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47347; -. DR STRING; 243273.MgenG_010200000740; -. DR EnsemblBacteria; AAC71319; AAC71319; MG_101. DR KEGG; mge:MG_101; -. DR PATRIC; 20009604; VBIMycGen98045_0111. DR OMA; WPANTRI; -. DR OrthoDB; EOG6C2WGS; -. DR BioCyc; MGEN243273:GH2R-104-MONOMER; -. DR Proteomes; UP000000807; 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 SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50949; HTH_GNTR; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 222 Uncharacterized HTH-type transcriptional FT regulator MG101. FT /FTId=PRO_0000050693. FT DOMAIN 8 77 HTH gntR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00307}. FT CONFLICT 27 48 WPANTRIFSERQLEIRFNSSRS -> HPYLLRTPTRNPFQL FT LTD (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 222 AA; 25998 MW; 9D06A5480E58124D CRC64; MKFGKEIAKK NQIIYRYIIL KIQSFEWPAN TRIFSERQLE IRFNSSRSQI RSVLATLLNK NIIRYTKNTP GYFVCKDVGF SFFHKTQDNL KVKYAKLSTL IKKLLSQDDA SVFANIDSTV HLDKFKGIEA KFFDENKKHF LNVCFFAKDD ILNILDENNL QQQFFREFAY NGIAIEKRHC VTSVDKESGC LVMYDMYYDD NDNFVVASKS NFLNPELKVI NA // ID Y115_MYCGE Reviewed; 157 AA. AC P47361; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 89. DE RecName: Full=Protein MG115; GN OrderedLocusNames=MG115; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the CinA 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; L43967; AAC71333.1; -; Genomic_DNA. DR RefSeq; WP_009885673.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47361; -. DR STRING; 243273.MgenG_010200000830; -. DR EnsemblBacteria; AAC71333; AAC71333; MG_115. DR KEGG; mge:MG_115; -. DR PATRIC; 20009634; VBIMycGen98045_0126. DR eggNOG; ENOG4107VSQ; Bacteria. DR eggNOG; COG1546; LUCA. DR KO; K03743; -. DR OMA; CVREMAL; -. DR OrthoDB; EOG61S359; -. DR BioCyc; MGEN243273:GH2R-119-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 3.90.950.20; -; 1. DR InterPro; IPR008136; CinA_C. DR Pfam; PF02464; CinA; 1. DR SUPFAM; SSF142433; SSF142433; 1. DR TIGRFAMs; TIGR00199; PncC_domain; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 157 Protein MG115. FT /FTId=PRO_0000156788. SQ SEQUENCE 157 AA; 16986 MW; 55402DF6BE559A98 CRC64; MFANLIAEKL QKLQLSVATA ESVTGGLLAH CLTSIDGASN YFNGGVIAYN NQVKINLLNV QSSTIANHGA VSSFCAREMA VGVKQKFQAD VGIACSGIAG SKAVENKAIG LLFFCIIIGN KAYDFEFEMN QNNRKDNIEL FTNKILESFH YLLTKLA // ID Y121_MYCGE Reviewed; 306 AA. AC P47367; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 85. DE RecName: Full=Uncharacterized protein MG121; GN OrderedLocusNames=MG121; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71339.1; -; Genomic_DNA. DR PIR; D64213; D64213. DR RefSeq; WP_009885677.1; NZ_AAGX01000002.1. DR STRING; 243273.MgenG_010200000860; -. DR EnsemblBacteria; AAC71339; AAC71339; MG_121. DR KEGG; mge:MG_121; -. DR PATRIC; 20009646; VBIMycGen98045_0132. DR eggNOG; ENOG41080EB; Bacteria. DR eggNOG; COG1079; LUCA. DR KO; K02057; -. DR OMA; LLNPQLW; -. DR OrthoDB; EOG6MSS3R; -. DR BioCyc; MGEN243273:GH2R-125-MONOMER; -. DR Proteomes; UP000000807; 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:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 306 Uncharacterized protein MG121. FT /FTId=PRO_0000210425. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 144 164 Helical. {ECO:0000255}. FT TRANSMEM 194 214 Helical. {ECO:0000255}. FT TRANSMEM 232 252 Helical. {ECO:0000255}. FT TRANSMEM 274 294 Helical. {ECO:0000255}. SQ SEQUENCE 306 AA; 33299 MW; 700A2479B676D67E CRC64; MLSLAQLESW FFIAPALLLA VLSGYLAERV GIINIAINGG MVFGGLFMAL LSYGFTNNLN QSAPSWSLFI TIPLSVLFSS VIGCLFALAA VKLRADHVIV GTGINLLASG ITLFISQNAA SLFSDTTLRV RYLFPIQTTV SIEAIGVFVF SLLLIGFVWY LMSFTKTGLR YRAVGENPNV IDTQGISVYK YQWIGAICSM MVAGLSGSLF VLSVSNFPFN SGDVNGLGFI AIAIMIISMW RIIPSIFIGL IFAYAYVFTN SQIGSNSNSY LLRTIPFIIS LLVMLLFGFL NVAPKNIGKH FDKGLR // ID Y187_MYCGE Reviewed; 585 AA. AC P47433; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Putative ABC transporter ATP-binding protein MG187; GN OrderedLocusNames=MG187; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71406.1; -; Genomic_DNA. DR PIR; G64220; G64220. DR RefSeq; WP_010869365.1; NC_000908.2. DR ProteinModelPortal; P47433; -. DR STRING; 243273.MgenG_010200003378; -. DR EnsemblBacteria; AAC71406; AAC71406; MG_187. DR KEGG; mge:MG_187; -. DR PATRIC; 20009814; VBIMycGen98045_0213. DR eggNOG; ENOG4108H07; Bacteria. DR eggNOG; COG3839; LUCA. DR KO; K10112; -. DR OMA; GVPEMNI; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-196-MONOMER; -. DR Proteomes; UP000000807; 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; -; 2. 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; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 2. 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 1 585 Putative ABC transporter ATP-binding FT protein MG187. FT /FTId=PRO_0000093241. FT DOMAIN 8 468 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 40 47 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 585 AA; 66949 MW; A447D78BE3C918BF CRC64; MANNKSAIEL KNIVVDFGES VAIDNINLSV EKHQLVSLLG PSGCGKTTTL AVIAGLIKPT SGQVLFNGYD VTKKPPQERK LGLVFQNYAL YPHMNVFENI VFPLYSDNSW KQAVLEKNSV ANHEINCLLL TSNGASVQEI DQLNKLFHDS IEKPKQIQYQ INDLNVSVFK NLNELTANLK LIPSKHQFAI TNLNKQTLKQ INELEAEFKT KWKLQKQTPI KSGVEHNAKL QAIKQHFSYE KQRLKKHYFK TKVELKQTLV ENLKLVKKAI SEQTKLIKQS SDYTKLKQLK RLIKVEPNQL KKQYKVFLNQ LIKNYSLKTD KLTDTQLNEI EQIKTRIVSI KQFINKTALE VANKLAITKI LTKRPDKISG GQQQRVAIAR AIVRRPKLLL MDEPLSNLDA KLRVQTRQWI RQFQQELQIT TVFVTHDQEE AMSISDVIVC MSTGKVQQIG TPSELYLKPA NEFVARFLGT PEMNIIECSV KNNQLFWNNH LLVTESFKLN VEKLLVGFRY EQLVVTTNKS SLQAKLINIE NLGKHLVATI SLFDTTLSMR LELNSHLKVG DSLNFIIKAN NLHFFDIDTK QRIEI // ID Y255_MYCGE Reviewed; 365 AA. AC P47497; Q49289; Q49297; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized protein MG255; GN OrderedLocusNames=MG255; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-365. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71475.1; -; Genomic_DNA. DR EMBL; U02174; AAD12457.1; -; Genomic_DNA. DR EMBL; U02164; AAD12446.1; -; Genomic_DNA. DR PIR; B64228; B64228. DR EnsemblBacteria; AAC71475; AAC71475; MG_255. DR KEGG; mge:MG_255; -. DR PATRIC; 20009994; VBIMycGen98045_0292. DR OMA; QWPILTT; -. DR OrthoDB; EOG66XBNF; -. DR BioCyc; MGEN243273:GH2R-278-MONOMER; -. DR Proteomes; UP000000807; 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 1 365 Uncharacterized protein MG255. FT /FTId=PRO_0000210489. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT TRANSMEM 151 171 Helical. {ECO:0000255}. FT TRANSMEM 187 207 Helical. {ECO:0000255}. FT CONFLICT 180 180 N -> KR (in Ref. 2; AAD12457). FT {ECO:0000305}. SQ SEQUENCE 365 AA; 42440 MW; 6609C2C8CA2CC5B7 CRC64; MESENQIAIL DYIFNQVNQP NQPKIVWFSG EGEDEKINFL IRLNDFFKPK FVENTNDSSF LLSFRNHVET KNSTPLTQAN FANIANKLLA VLFGSLQWKQ LNKPTGNWFL VILFLALLWL RQCWLKLQLT KISKFVNQKG ILSFIKQQWP ILTTLVTVGT TLGTPVFSLT IAQQDGIKQN AGNDVFIFLI IFSVFSISLG LVSSLIFLVS SLFSIRQKKT LDALDKVLSK FIDKYFFLDE KEIKKQLKYQ FKNNGVCFFY GFDFDQAEFL EQSMNLMLLL KQTNCFILVG CKESEMTLIK NKIEPNINLK QNSFYLDLSN EISQVEQISK FNLLFRQLRL SSELFYLEDF FDYLTTAKQI VNFLF // ID Y277_MYCGE Reviewed; 970 AA. AC Q49409; Q49253; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Uncharacterized protein MG277; GN OrderedLocusNames=MG277; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 624-678. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71499.1; -; Genomic_DNA. DR EMBL; U02116; AAD12390.1; -; Genomic_DNA. DR PIR; F64230; F64230. DR RefSeq; WP_010869403.1; NC_000908.2. DR ProteinModelPortal; Q49409; -. DR EnsemblBacteria; AAC71499; AAC71499; MG_277. DR KEGG; mge:MG_277; -. DR PATRIC; 20010054; VBIMycGen98045_0319. DR KO; K12257; -. DR OMA; ALTFEYK; -. DR OrthoDB; EOG6HTNSM; -. DR BioCyc; MGEN243273:GH2R-306-MONOMER; -. DR Proteomes; UP000000807; 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 1 970 Uncharacterized protein MG277. FT /FTId=PRO_0000210502. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 515 535 Helical. {ECO:0000255}. FT TRANSMEM 537 557 Helical. {ECO:0000255}. FT TRANSMEM 558 578 Helical. {ECO:0000255}. FT TRANSMEM 614 634 Helical. {ECO:0000255}. FT TRANSMEM 645 665 Helical. {ECO:0000255}. FT TRANSMEM 726 746 Helical. {ECO:0000255}. FT TRANSMEM 762 782 Helical. {ECO:0000255}. FT TRANSMEM 789 809 Helical. {ECO:0000255}. FT TRANSMEM 816 836 Helical. {ECO:0000255}. FT TRANSMEM 877 897 Helical. {ECO:0000255}. FT TRANSMEM 903 923 Helical. {ECO:0000255}. FT COMPBIAS 50 53 Poly-Thr. FT COMPBIAS 370 382 Poly-Asn. FT CONFLICT 673 678 SGANWK -> QVQMKA (in Ref. 2; AAD12390). FT {ECO:0000305}. SQ SEQUENCE 970 AA; 108164 MW; F106CDFCC9BD44FF CRC64; MRFKKRFSLD WILKIGTILG LVCLGLFGVI FGSYKLLNDS RLGAVFNGST TTTVYFLNHK STNNTSLDPQ QTKPTNGIEN ITNIDSFLDG VEKSYANSLF IQGFSSVNIT KNTNDKTASE LDNIDKSWLV NGGLPSVTLT FEQNREQAKT RQRKRQVDAQ VRRNAISSVE HNYQLSLETT DGVVLFDSLD NNFINASIRA VVPQNTSVNS ALTFEYKLNK NVVTKESLHT DFLDFINSKN LSSSDYNTGN GQASVEGNGK FFKQNANGTS SSGNKTLVLW KDKQGALNYV RNIFNVVEGS SDYLTFNERE KSLWEFLHAK GSFASGDNLF LNTDANGASP IKKASDITLK NLYYIYAAPN HFSAVASNSN DNNNQNNNNN NNSSDVITVS NSADTRKLRS ADSSGFSGLF HNYIISEIRT EDPVSKTGDP VKINPTLQSF LDTNNQRIEY GGNIKFQVGN FLSSDGTYTP PNFVTAATVK ELLTNPFPTA ATIATAKTSL VNAPLANTIT DVSNFASSFI AFGIIVLIAA VLLTLRYKLL GLYKALALGL SVVSSLVIFS AVGGVVDVFS FVGIFFVIAI NLINLLNLGE LFLRNIRNNA SIIESWKLCL KRSFFANLEF HITWLISALV VIYLSNYQVQ QLANLMAISA ITSYFFSYGI SIVLISLFVS SESGANWKLF LYQKDAKALT KTSSNYSLLS STSDLNTDFF ITKNQHDFFL KNNWKFLFVW LILLAIGVVM LVLYLVQPNL LGEFLAADVE SSNGIIAGIG IVSLLYLAYC LIRYGVAYCL SYLVSFILLC SGLFAVMYLT NYLFSIDQST IQLITFVYLF WLFFAAKVSQ TTTWTYFYWF KRSLKDKVFI KNLFNDNFNS QWKIDLIESS SLVFIFIIYS GFNFGGIDGN FNLVIFYLIA IVGLFDVATA FLPMFCFGLI NGWLSPFNYV HSRLSLKHKK HPFKEIDQIE EQLIAGINSF // ID Y306_MYCGE Reviewed; 393 AA. AC P47548; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=Uncharacterized protein MG306; GN OrderedLocusNames=MG306; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71528.1; -; Genomic_DNA. DR PIR; H64233; H64233. DR RefSeq; WP_010869420.1; NC_000908.2. DR STRING; 243273.MgenG_010200002519; -. DR EnsemblBacteria; AAC71528; AAC71528; MG_306. DR KEGG; mge:MG_306; -. DR PATRIC; 20010142; VBIMycGen98045_0357. DR eggNOG; ENOG4107I1S; Bacteria. DR eggNOG; COG0392; LUCA. DR KO; K07027; -. DR OMA; HIKYVEE; -. DR OrthoDB; EOG6J74S4; -. DR BioCyc; MGEN243273:GH2R-342-MONOMER; -. DR Proteomes; UP000000807; 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; IPR022791; L-PG_synthase/AglD. DR Pfam; PF03706; LPG_synthase_TM; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 393 Uncharacterized protein MG306. FT /FTId=PRO_0000210524. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TRANSMEM 56 76 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 131 151 Helical. {ECO:0000255}. FT TRANSMEM 176 196 Helical. {ECO:0000255}. FT TRANSMEM 253 273 Helical. {ECO:0000255}. FT TRANSMEM 289 309 Helical. {ECO:0000255}. FT TRANSMEM 349 369 Helical. {ECO:0000255}. SQ SEQUENCE 393 AA; 45750 MW; D740FDA979EC364A CRC64; MAKLTTNTFF NTKNIVAFSF FLVFLIVISV IVTIFFLGVS VDDVKTIITA INYQNWGWIF VVILGFLVSV LWNVIINWWV SRRFCFYASW WEWLLFGFVV QFFQIVTPLS LGQDPFRLYW FIKKGMKKQT AVLIVTSTGA FWNLSQALIT WPSFFVLSKN YQLLANNHNS FVSYWLSLTG MIFDVVVAIL FIVIAFNKKM HVLIYSLVNQ FRKWLKRPYL TKEQIYQRFI EKAEFNKLYG IEMRRWGLTI FKLLANMVVA IVSYFSLFGV FMITKTVNTT NNVIDQYSLI DLFNITNIAV TASNFIPVAS GEGATQFVMT SFLNAFKPTD QFLHDQIKDG VFLWRLLSVY LPAIFTGICF VVWIVQVIWE FKKTVNVPLK TVNTVSLETK KDK // ID Y320_MYCGE Reviewed; 286 AA. AC P47562; Q49508; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 75. DE RecName: Full=Uncharacterized protein MG320; GN OrderedLocusNames=MG320; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-260. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71542.1; -; Genomic_DNA. DR EMBL; U01700; AAB01012.1; -; Genomic_DNA. DR PIR; D64235; D64235. DR RefSeq; WP_010869429.1; NZ_AAGX01000013.1. DR STRING; 243273.MgenG_010200003023; -. DR EnsemblBacteria; AAC71542; AAC71542; MG_320. DR KEGG; mge:MG_320; -. DR PATRIC; 20010170; VBIMycGen98045_0371. DR OMA; NFEANDI; -. DR OrthoDB; EOG61CM8D; -. DR BioCyc; MGEN243273:GH2R-356-MONOMER; -. DR Proteomes; UP000000807; 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 1 286 Uncharacterized protein MG320. FT /FTId=PRO_0000210536. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 99 119 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. FT TRANSMEM 169 189 Helical. {ECO:0000255}. FT TRANSMEM 205 225 Helical. {ECO:0000255}. FT TRANSMEM 254 274 Helical. {ECO:0000255}. FT CONFLICT 156 156 L -> H (in Ref. 2; AAB01012). FT {ECO:0000305}. FT CONFLICT 258 260 FGA -> LGL (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 286 AA; 32450 MW; 2F5BEDE951298456 CRC64; MINSTKGYID QNGLAAKQFV QTKQLSVIRL TFMVAAFGIF FIFLVALTVQ QLLSRSTLID LASDFRTLST IAVITSFVSL ILYFVTAFKL RNPNTSLTWF WALIITDVIS YGITLGILLT LATTFSKQVN FEANDIVYAF LGASLVFGSV WGLSALPSQK RRYQQTQTLF HILLWAFVIS IVASLLSFIL NFTVFASTTN LLDRIIPGLS LIVGGIFSLI SVYFVSLQIR NEQDLIKYYE SEDYEMARRQ SWRSALFFGA WLISSFMNLV YFILRIILIT KNFSRV // ID Y342_MYCGE Reviewed; 168 AA. AC P47584; Q49340; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=Uncharacterized protein MG342; GN OrderedLocusNames=MG342; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-128. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71567.1; -; Genomic_DNA. DR EMBL; U02231; AAA03383.1; -; Genomic_DNA. DR PIR; H64237; H64237. DR RefSeq; WP_009885799.1; NZ_AAGX01000006.1. DR ProteinModelPortal; P47584; -. DR STRING; 243273.MgenG_010200001813; -. DR EnsemblBacteria; AAC71567; AAC71567; MG_342. DR KEGG; mge:MG_342; -. DR PATRIC; 20010250; VBIMycGen98045_0402. DR eggNOG; ENOG4105Q8W; Bacteria. DR eggNOG; ENOG4111WMJ; LUCA. DR OMA; PEINGYM; -. DR OrthoDB; EOG6SNDXM; -. DR BioCyc; MGEN243273:GH2R-392-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR005025; FMN_Rdtase-like. DR Pfam; PF03358; FMN_red; 1. DR SUPFAM; SSF52218; SSF52218; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 168 Uncharacterized protein MG342. FT /FTId=PRO_0000210549. FT NP_BIND 119 126 ATP. {ECO:0000255}. FT CONFLICT 23 23 F -> M (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 168 AA; 19128 MW; A04F2492265F5DA6 CRC64; MSKDQKSLIL MLSNSQHSIN RKFANELKHS LSCELIELKD YQVDFYSVDL EATNFPDKIK TLVRKIKEHS NLIFVTPEHN GFIPAFAKNI IDWMTRDEQY GRNQFLKGLN GVICCVTPAT AGGGKTVLEL LDKFLSFSGL NVKGTVLVNG YHENFDFKPF IEQVKKLI // ID Y350_MYCGE Reviewed; 311 AA. AC P47592; Q49205; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 60. DE RecName: Full=Uncharacterized protein MG350; GN OrderedLocusNames=MG350; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 91-160. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71575.1; -; Genomic_DNA. DR EMBL; U01731; AAC43209.1; -; Unassigned_DNA. DR PIR; G64238; G64238. DR RefSeq; WP_010869445.1; NC_000908.2. DR EnsemblBacteria; AAC71575; AAC71575; MG_350. DR KEGG; mge:MG_350; -. DR PATRIC; 20010272; VBIMycGen98045_0411. DR OMA; DLLMINI; -. DR OrthoDB; EOG6PZXKW; -. DR BioCyc; MGEN243273:GH2R-402-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 311 Uncharacterized protein MG350. FT /FTId=PRO_0000210555. FT CONFLICT 91 91 S -> G (in Ref. 2; AAC43209). FT {ECO:0000305}. FT CONFLICT 159 160 KI -> RY (in Ref. 2; AAC43209). FT {ECO:0000305}. SQ SEQUENCE 311 AA; 37008 MW; 51F9F4CC102C5584 CRC64; MKISPDQKDK KSLFKKHFAY LKLTEKELND PKIQTLLEVA WNHFDQCRKI KERRCSNKGD IHLQAVREWL PWEFNANQLK KNSTKETTQV SENEFMGNVM LMQTICPKLV NKANWFDLTY ERFIVTKPNW FKYMDLIPMI QNLPVTPSDK NSFGYAYKKI SNLFETEKKT KKRIFFFNLQ KNNINNMAAC MLTCEIAKKN IKVALIYCEE FVSRYDKSYW KVDDDLNLLD EAKVIIFIGL GQESFHNKNY ILFMTRLFIN CFLKRKDVFF FSTTYSDGNG LIQTFKNQII SSANWVKHFF EQLNDLLMIN I // ID Y406_MYCGE Reviewed; 113 AA. AC Q49431; Q49202; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 72. DE RecName: Full=Uncharacterized protein MG406; GN OrderedLocusNames=MG406; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-113. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71634.1; -; Genomic_DNA. DR EMBL; U01728; AAC43206.1; -; Unassigned_DNA. DR PIR; I64244; I64244. DR EnsemblBacteria; AAC71634; AAC71634; MG_406. DR KEGG; mge:MG_406; -. DR OMA; ARYLIYL; -. DR OrthoDB; EOG6G4VVV; -. DR BioCyc; MGEN243273:GH2R-463-MONOMER; -. DR Proteomes; UP000000807; 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 1 113 Uncharacterized protein MG406. FT /FTId=PRO_0000210594. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 45 65 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. SQ SEQUENCE 113 AA; 12931 MW; 64421B1BB9C884C2 CRC64; MLPLPFAVLN SLSVLRLASF FASLKNVKKQ KAVSFFAFFF TARYLIYLIP VIISFVVTPS IFNTIATIIS TLFFPILNLV LSFVWLPLEY FFINLISKSK RKHVATGDSF KRN // ID Y414_MYCGE Reviewed; 1036 AA. AC P47653; P47654; Q49457; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 78. DE RecName: Full=Uncharacterized protein MG414; GN OrderedLocusNames=MG414; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-146 AND 733-833. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MG414/MG415 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; L43967; AAC71641.1; -; Genomic_DNA. DR EMBL; U01695; AAB01008.1; -; Genomic_DNA. DR EMBL; U01804; AAD12330.1; -; Genomic_DNA. DR PIR; H64245; H64245. DR RefSeq; WP_010869473.1; NC_000908.2. DR STRING; 243273.MgenG_010200000415; -. DR EnsemblBacteria; AAC71641; AAC71641; MG_414. DR KEGG; mge:MG_414; -. DR PATRIC; 20010418; VBIMycGen98045_0482. DR OMA; VDGYESE; -. DR OrthoDB; EOG6W19D7; -. DR BioCyc; MGEN243273:GH2R-470-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 1036 Uncharacterized protein MG414. FT /FTId=PRO_0000210598. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 1004 1024 Helical. {ECO:0000255}. FT CONFLICT 733 736 LEPT -> SRAS (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 1036 AA; 123180 MW; 12A21F00F686A141 CRC64; MRSYLFIPLL VSFLFPVALA NASLEKNLVD TNLYLSPNTI QNRSYTAGFN LKNDYFRKSF NFDNEVIQRP NQNNYFAKTY SNEWSELVNK YSDNYKQIIR DNNFHWYNNI YYLKNIKLKI ESSYIAHAFS STFRYPGIRN SWSSDIHSEQ RFYFHSQAIS NFFPRDGHTN EKWTEVPSRN IEITGTNPDG SWNKSWYKPD NPYFWDLTKP SHKKAYFIEA KFVHMWGSTL RMIKPTPEDV IRNIKWLRKG NNGNYVIDFN APMWYYLGQE SRGFFADWKN NIFVAPDFWW GLAMTPIRAY RFWWDLELVK VPPVFEQNNA QWNEPFPGRS SWFFSINSNK QVDAHWMSIN EFKEKMKKDR KIIEAFTNNR EITQTILRLG NGLVVRPETE DSRREAFNSK WDIFKHTPIL PEQEVVHHQI SFYLRQNNPD EVLPISFSNL SKLWISQLEF DINSLVSQTE KTLNKETIGT KIKPTIKFKD KFINAIKEVS LINQRIDESI DKNEALKSFN ISTNNQSNFY PNLDYLYNLL QMSPNNKEEL FFIRNLPRMV KTIFDRSTLT VKVKIGNSVN EITLLRNNKN YFDLSSIEEF LTEKQKADNE MNIEFLALNF FVDGYESENI SNYSVEPLFD SIKKLSTIKR TKDGFEYKFK YRKDFNEQRW IAKDFRIPLN KNVQNFNVAE LKKRNEKFND YEKRQMAFII KNSFKSKDKN IDLDINSNSL TFVDNPKKYF KHLEPTNEKK GIFYVLAEIN NSNELFKYGS ESDSEIIKDK MYFLSQNQKN PKLRTYLFKF HTNKLFVDKN DLGFKLEKDK VFLSVDNLKI AELDLKSSSF KFLEDYQLDF HEPFSLNDEQ LLVDKLNITL SEKRLQTTKN VRFNLKNKFI NIHLVENKNQ FNLVFDVDVR SKKLFIKGVN NDNQVFSISY DLKITNNQTL LIVDANGFDN SIWFDITSEN QTQLFKALSF YLKQNNLQFK RVPDFNLKSQ DKSYEVDKLE KNEIKKQDTN VELILWVIFG IIISLMISSA VLFLKWRKKK IVKKRN // ID Y459_MYCGE Reviewed; 169 AA. AC Q49436; Q49199; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 78. DE RecName: Full=Uncharacterized protein MG459; GN OrderedLocusNames=MG459; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-110. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC72479.1; -; Genomic_DNA. DR EMBL; U01725; AAC43201.1; -; Unassigned_DNA. DR PIR; G64250; G64250. DR RefSeq; WP_009885572.1; NZ_AAGX01000001.1. DR ProteinModelPortal; Q49436; -. DR STRING; 243273.MgenG_010200000130; -. DR EnsemblBacteria; AAC72479; AAC72479; MG_459. DR KEGG; mge:MG_459; -. DR PATRIC; 20010512; VBIMycGen98045_0529. DR eggNOG; COG0245; LUCA. DR OMA; DYKHAIF; -. DR OrthoDB; EOG6J48RZ; -. DR BioCyc; MGEN243273:GH2R-512-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:InterPro. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1330.50; -; 1. DR InterPro; IPR003526; MECDP_synthase. DR Pfam; PF02542; YgbB; 1. DR SUPFAM; SSF69765; SSF69765; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 169 Uncharacterized protein MG459. FT /FTId=PRO_0000210627. SQ SEQUENCE 169 AA; 19215 MW; F60636F17BAFA5AC CRC64; MQLRVGLGSK KYHIKLRKES KNKFWLGGVD FENSKYIYDL ENSDEVSDVI QLAVADALFG ATALGDGHIV FNKGKSTVQF KGTAKKEAPR VLARTYNFIR KNWIINNIDI SLEIPQEQKV DDYKHAIFAF ICSALRISEL TINLKVRKPL DSNEINCLAV VLVERQKTK // ID Y140_MYCGE Reviewed; 1113 AA. AC P47386; Q49203; Q49283; Q49445; Q49472; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized ATP-dependent helicase MG140; DE EC=3.6.4.-; GN OrderedLocusNames=MG140; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-267. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-267; 294-394 AND 999-1100. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase 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; L43967; AAC71358.1; -; Genomic_DNA. DR EMBL; X61512; CAA43726.1; -; Genomic_DNA. DR EMBL; U01729; AAC43207.1; -; Unassigned_DNA. DR EMBL; U01742; AAD10552.1; -; Genomic_DNA. DR EMBL; U02156; AAD12438.1; -; Genomic_DNA. DR PIR; E64215; E64215. DR RefSeq; WP_010869351.1; NC_000908.2. DR ProteinModelPortal; P47386; -. DR EnsemblBacteria; AAC71358; AAC71358; MG_140. DR KEGG; mge:MG_140; -. DR PATRIC; 20009708; VBIMycGen98045_0160. DR OMA; NEWRERN; -. DR OrthoDB; EOG6G4VR9; -. DR BioCyc; MGEN243273:GH2R-147-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR025103; DUF4011. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13195; DUF4011; 1. DR SUPFAM; SSF52540; SSF52540; 3. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 1113 Uncharacterized ATP-dependent helicase FT MG140. FT /FTId=PRO_0000080728. FT NP_BIND 313 320 ATP. {ECO:0000255}. FT CONFLICT 267 267 D -> R (in Ref. 2 and 3). {ECO:0000305}. FT CONFLICT 394 394 L -> W (in Ref. 3). {ECO:0000305}. FT CONFLICT 1092 1100 PIGVISKIR -> QLGWFLKSD (in Ref. 3). FT {ECO:0000305}. SQ SEQUENCE 1113 AA; 130580 MW; FF0C51F926725D3F CRC64; MNDWQWLKNR LVNSKTKSVS FWLPQTSSNI IDIAELIKCC SELKNTSING LIDFLNQQDK LEFNLTRLKE IDVEDGKQLF GIETSVYKHF QNEIARFYKQ VNKHFRETGS ESLFLALPVI EGINEFNDIF RAPLLYVGVK LKVSPRFERF WLEINKEEIF LNPTIIGVET NKRNSLFKNN YDTTKIDVND ALKVFSELEY EFRMPLTSEL KSFSKKAKSD FNTEKRTNYL INNVLLGIFD VKGDQLFQNF NEILNTDPDV LDELLKDRRD LLLENREFRE QFDLKDTYLF SHLDIYQQYA VKQALLGDLI IEGPPGTGKS ETIVNILVNL VLNNKKVLFV SEKVTALDVV YNRLGSFKHI ALFNASVAAE KKRFYNQFAE FETYFTTYFS KKDLDATLPT FEGKWVDDIL GAFQALQALY DTKINSGENL FSFKEIVSSF QMLDASYIKI KEYERFDEWV RVFSNPLWLE KHLSYQELKK ELSQRWNGID NFYQLQSLLN QTKKRKVLNY VLEHFEQFNT VISPKHVLFY KPSNKSQLLL KQLKQDVEQY TSLQRFQSPT KFETIKLNFI NQVNENPTPW FFSWFIQFHA KPLLEKLVSF ESNIIKTKQA YLNGIESYVA SCKKLLKTTI LNNFFQLYQT NKDELLEICR QAKNPVLKEI TWWFKKHFEL LKKLFPVHIM TLESAATLTP NQRGLYDYVV IDEASQVFLE RAIPILFRAD KYIIAGDTKQ LKPANFFQSR AEYDVDEEFE DGNIEAAVHS SSLLHFLKNR SRILTLLKFH YRSDSADLIA FTNNRIYDNE LIFMNKANAD QRVFIVHDVI DGIWKNNRNL QEARDVVQRL EQLTTTNDYK KSLGVICFNK NQADLIEYLI DKQNNPLLNE WRERQNDVGE YEGLFVKNIE NVQGDERDII IFSLGYDRSV NSYGPISKQG GENRLNVAIT RAKQRIELFK TNRGEDYNGL SSSSLGSKLL VEYLLYCEAM AKNQGEKITF QAVKRKETKA KYELAVENDF FNQLQAIFGG EFEIKRNVNE GAYFFSFVFY FNNIPYLAID FNIPIPTSRK QVMEGILYRE QFLKKRQWNL INIWIDEWKL NPIGVISKIR SSLAVHQNQH EEI // ID Y144_MYCGE Reviewed; 279 AA. AC P47390; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 75. DE RecName: Full=Uncharacterized protein MG144; GN OrderedLocusNames=MG144; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-140. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71362.1; -; Genomic_DNA. DR EMBL; U02121; AAD12395.1; -; Genomic_DNA. DR PIR; I64215; I64215. DR RefSeq; WP_009885830.1; NZ_AAGX01000007.1. DR STRING; 243273.MgenG_010200002079; -. DR EnsemblBacteria; AAC71362; AAC71362; MG_144. DR KEGG; mge:MG_144; -. DR PATRIC; 20009718; VBIMycGen98045_0165. DR OrthoDB; EOG6W724W; -. DR BioCyc; MGEN243273:GH2R-152-MONOMER; -. DR Proteomes; UP000000807; 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 1 279 Uncharacterized protein MG144. FT /FTId=PRO_0000210440. FT TRANSMEM 156 176 Helical. {ECO:0000255}. FT TRANSMEM 202 222 Helical. {ECO:0000255}. FT TRANSMEM 237 257 Helical. {ECO:0000255}. SQ SEQUENCE 279 AA; 31717 MW; 8BB3842C99C2CC41 CRC64; MDPQNKSPKP QVKSTRLVVK KQPAGVVFPK LSIPVNDFEK TVTLTRAQKK EAKLLKKAQR KANKLNNKQD STFFNSASGE TNNTILPPGV KNQADNKTNR FSKFISFFTS SKNKQPDEIT ERLVDDPTVK NRFSAFNKKL IWVLKDKKLR ARAWKIVGYT NLVIVAFFAG LLAVMNKFIT LSSVEYPAIA LQLPINNALW GISIFVISIV TLPFWTMFIL FLMGVKDVRT SRSIHYFIWI VLIINVVLLL VSCLLMIAAY AHLDGYNIWR NLESLNPNN // ID Y207_MYCGE Reviewed; 163 AA. AC P47449; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-MAY-2016, entry version 93. DE RecName: Full=Putative metallophosphoesterase MG207; DE EC=3.1.4.-; GN OrderedLocusNames=MG207; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CC YfcE family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC71425.1; 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; L43967; AAC71425.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; P47449; -. DR STRING; 243273.MgenG_010200001387; -. DR EnsemblBacteria; AAC71425; AAC71425; MG_207. DR KEGG; mge:MG_207; -. DR PATRIC; 20009868; VBIMycGen98045_0239. DR eggNOG; ENOG41084IK; Bacteria. DR eggNOG; COG0622; LUCA. DR KO; K07095; -. DR OMA; TIANNKM; -. DR OrthoDB; EOG6D2M09; -. DR BioCyc; MGEN243273:GH2R-216-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016787; F:hydrolase activity; 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; IPR020935; PdiEstase_YfcE_CS. 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. DR PROSITE; PS01269; UPF0025; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 163 Putative metallophosphoesterase MG207. FT /FTId=PRO_0000155609. SQ SEQUENCE 163 AA; 18865 MW; AC7BC01F40AB0753 CRC64; MIKVLVIADT HGQNQRWIEL KNYHNPDVII HAGDHMTTKQ FMDQNATFWV AGNNDSIGNE IEIFQLGQIN FVLMHGHQAP RDNLKKWYQL LVLKAQQYPC DVLIFGHSHI EYTNKINMIQ LINPGSLQLP RNQTNTPSYC TFIVNKDELT DLTIHYYQAS KVS // ID Y236_MYCGE Reviewed; 140 AA. AC P47478; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 72. DE RecName: Full=Uncharacterized protein MG236; GN OrderedLocusNames=MG236; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71457.1; -; Genomic_DNA. DR PIR; A64226; A64226. DR RefSeq; WP_009885773.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47478; -. DR STRING; 243273.MgenG_010200001607; -. DR EnsemblBacteria; AAC71457; AAC71457; MG_236. DR KEGG; mge:MG_236; -. DR PATRIC; 20009954; VBIMycGen98045_0273. DR eggNOG; COG0735; LUCA. DR OMA; NDFYIVA; -. DR OrthoDB; EOG6FBX26; -. DR BioCyc; MGEN243273:GH2R-258-MONOMER; -. DR Proteomes; UP000000807; Chromosome. 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 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Uncharacterized protein MG236. FT /FTId=PRO_0000210473. SQ SEQUENCE 140 AA; 16520 MW; D3E368F414942BD1 CRC64; MLTSYVKVLE QNNLRLTKPR IALLKCLIEH QDWHNLSQIK THLDLANQPS TLASIYNNLR ILAKLKLINI FVDPERFETY YCLRHAEHNH IYLFDEVKQQ FFTLPLTDGQ IKTLLETQNH TSKVKLNDFY IVARGEINND // ID Y237_MYCGE Reviewed; 294 AA. AC P47479; Q49224; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 67. DE RecName: Full=Uncharacterized protein MG237; GN OrderedLocusNames=MG237; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-294. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71458.1; -; Genomic_DNA. DR EMBL; U01774; AAD10594.1; -; Genomic_DNA. DR PIR; B64226; B64226. DR RefSeq; WP_009885774.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47479; -. DR SMR; P47479; 5-290. DR STRING; 243273.MgenG_010200001612; -. DR EnsemblBacteria; AAC71458; AAC71458; MG_237. DR KEGG; mge:MG_237; -. DR PATRIC; 20009956; VBIMycGen98045_0274. DR OMA; SELANDQ; -. DR OrthoDB; EOG66MQNX; -. DR BioCyc; MGEN243273:GH2R-259-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 1.10.472.40; -; 1. DR Gene3D; 1.20.1480.10; -; 1. DR Gene3D; 3.30.1790.10; -; 1. DR InterPro; IPR024503; DUF3196. DR InterPro; IPR023344; Uncharacterised_MG237_C. DR InterPro; IPR023402; Uncharacterised_MG237_central. DR InterPro; IPR023403; Uncharacterised_MG237_N. DR Pfam; PF11428; DUF3196; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 294 Uncharacterized protein MG237. FT /FTId=PRO_0000210475. SQ SEQUENCE 294 AA; 34572 MW; 23712137412C5512 CRC64; MINKPNQFLN HLDGLKQHFS DYDSLQKSFK KYLSENQTEL NNFFFNQFEK IIVLVKKKEF KTAQERCEEE LATPYFSKPL VGFFQSLLQL INHDLIEQKN QQLANMSCEK IVEMVLSDYP NKLNLIHYLL AKEASFVNPN LLQRMTFVLT DLELLELKRF SFFKALNQIP AFKNHKVTYF NSKLKQKFVI TLGEFAFPQT DKTKQFFQQL IKKVSQLFLK EPVSCEFAYE IIDALLVSFF PLHPNLEVNH LAKKIHQYVS KIVINEVVDL KDPTTKLIVD TLYEQLDRAI GEEN // ID Y248_MYCGE Reviewed; 218 AA. AC P47490; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 72. DE RecName: Full=Putative tRNA (adenine-N(1)-)-methyltransferase MG248; DE EC=2.1.1.-; GN OrderedLocusNames=MG248; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L- CC homocysteine + tRNA containing N(1)-methyladenine. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TrmK 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; L43967; AAC71468.1; -; Genomic_DNA. DR PIR; D64227; D64227. DR RefSeq; WP_009885786.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47490; -. DR STRING; 243273.MgenG_010200001697; -. DR EnsemblBacteria; AAC71468; AAC71468; MG_248. DR KEGG; mge:MG_248; -. DR PATRIC; 20009978; VBIMycGen98045_0285. DR eggNOG; ENOG4108V39; Bacteria. DR eggNOG; COG2384; LUCA. DR KO; K06967; -. DR OMA; WTITTET; -. DR OrthoDB; EOG6716R9; -. DR BioCyc; MGEN243273:GH2R-270-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR006901; TrmK. DR Pfam; PF04816; TrmK; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 218 Putative tRNA (adenine-N(1)-)- FT methyltransferase MG248. FT /FTId=PRO_0000210487. SQ SEQUENCE 218 AA; 25188 MW; E213395E1B87CB7D CRC64; MKKRISTIAN LVQSFNPKLV YDIGCDHSYL TSYLIKTNQN LTIVNSDISK NALLSNYQKF KNNNNIHFFV SDGFNNLPEL NINPKIGVIA GLGGLKIINI ISQKENFINR FVIQPQSNLI ELRSFLSLNS WDIVNETLVQ DREFIYPILV IEKLKKPFKL TKELVILGPK LINFKDKHCL MKHYQCLLRV YQPKQKPSLM DLKIIETLNK IITSYESS // ID Y252_MYCGE Reviewed; 242 AA. AC P47494; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 85. DE RecName: Full=Uncharacterized tRNA/rRNA methyltransferase MG252; DE EC=2.1.1.-; GN OrderedLocusNames=MG252; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase TrmH 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; L43967; AAC71472.1; -; Genomic_DNA. DR PIR; H64227; H64227. DR RefSeq; WP_010869393.1; NC_000908.2. DR ProteinModelPortal; P47494; -. DR STRING; 243273.MgenG_010200001722; -. DR EnsemblBacteria; AAC71472; AAC71472; MG_252. DR KEGG; mge:MG_252; -. DR PATRIC; 20009986; VBIMycGen98045_0289. DR eggNOG; ENOG4105C2N; Bacteria. DR eggNOG; COG0566; LUCA. DR KO; K03218; -. DR OMA; WIYYASE; -. DR OrthoDB; EOG6GBMDM; -. DR BioCyc; MGEN243273:GH2R-274-MONOMER; -. DR Proteomes; UP000000807; Chromosome. 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; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. 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 SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00186; rRNA_methyl_3; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 242 Uncharacterized tRNA/rRNA FT methyltransferase MG252. FT /FTId=PRO_0000159833. FT BINDING 198 198 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 218 218 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000250}. FT BINDING 227 227 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000250}. SQ SEQUENCE 242 AA; 27708 MW; F4325324663FB766 CRC64; MKKPRQQSCL FGVKAFEEAI NNQVHIKLVN ISIRHKKLIP LIEAKKINFQ IHSTNWFNNQ YRDINHQELV AVLDTNQLLI PLDQLVKVVE NKKCSTLVML DEIQDPYNFG AILRTCLASE VDGIIFKKNN QVPINNTVMK TSMGSVFYQN LVQVANLSYT ITKLKEIGFW TVVSTLDPIW KPIDYRKVDF AKKILIVGNE DRGVNQLITK NADCRIKIPM NNKINSLNVS VALGIILFAW KN // ID Y269_MYCGE Reviewed; 340 AA. AC Q49407; Q49328; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 63. DE RecName: Full=Uncharacterized protein MG269; GN OrderedLocusNames=MG269; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SEQUENCE CAUTION: CC Sequence=AAD12510.1; 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; L43967; AAC71491.1; -; Genomic_DNA. DR EMBL; U02215; AAD12510.1; ALT_INIT; Genomic_DNA. DR PIR; G64229; G64229. DR RefSeq; WP_009885900.1; NZ_AAGX01000009.1. DR STRING; 243273.MgenG_010200002624; -. DR EnsemblBacteria; AAC71491; AAC71491; MG_269. DR KEGG; mge:MG_269; -. DR PATRIC; 20010036; VBIMycGen98045_0310. DR OMA; HAIKEAN; -. DR OrthoDB; EOG63VBVS; -. DR BioCyc; MGEN243273:GH2R-297-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 340 Uncharacterized protein MG269. FT /FTId=PRO_0000210498. SQ SEQUENCE 340 AA; 39662 MW; 3921FE1F81501CC4 CRC64; MNNFDYYRDF DDFQRRETIN FFLAKFPFAS KAQLDVFLEQ AKTAYVKLRT SNPKNVDWNQ MLVLLLKKFG PEARSEKERL KRILSLQEQL KVRLEGEINR QVQQNSELFS QLKQSESEII QMQQLVEAKE HQIEALNKQL HAIKEANKKL IEEHESINVE ELLKEYEVQC NEAIYKRDQH IQTVFEDKLA LKDGEISETQ SLLKTAEKEK QALKKAYKLV VNSLQKHQKL TTEIEIDFTK LDEIIATIFD ETKNPKTGFT NFIKQFEKTK AKLTKKIAEI TKLDHSTPTN YQQETPASQQ QLDQENEPIK PSKKSNSSSL PRGTTQPKSN SINRVSKLID // ID Y280_MYCGE Reviewed; 265 AA. AC P47522; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-MAY-2016, entry version 74. DE RecName: Full=Uncharacterized protein MG280; GN OrderedLocusNames=MG280; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC71502.1; 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; L43967; AAC71502.1; ALT_INIT; Genomic_DNA. DR PIR; I64230; I64230. DR RefSeq; WP_009885910.1; NZ_AAGX01000009.1. DR EnsemblBacteria; AAC71502; AAC71502; MG_280. DR KEGG; mge:MG_280; -. DR PATRIC; 20010060; VBIMycGen98045_0322. DR OMA; HEVTFRI; -. DR OrthoDB; EOG6P8TT4; -. DR BioCyc; MGEN243273:GH2R-309-MONOMER; -. DR Proteomes; UP000000807; 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; IPR019449; FMP27_WPPW_dom. DR InterPro; IPR030940; MG279/MG280. DR Pfam; PF10359; Fmp27_WPPW; 1. DR TIGRFAMs; TIGR04527; mycoplas_twoTM; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 265 Uncharacterized protein MG280. FT /FTId=PRO_0000210506. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 201 221 Helical. {ECO:0000255}. SQ SEQUENCE 265 AA; 29566 MW; BB2BA19548B4C71D CRC64; MVIFINRFSK TILLFFGMLV FVFLLGFGIT ALYFRSTAAN LYVQARNSID SSFNSAKAFA NALANSANQF SKSSITNNLD QVKKDLEQSL QKVDEYKKNL ESQNNLGNIS QEKIRELDAT KKDLENSKTQ LDNFKNNLDK NGTASSSPSV KKQATADGVI SAVSEFSTQA QSIVSSYEKI KNNIPSSEQF NNYYDVTMIT IVAVSGGMLA ILITTIVFSF LTSKKRGLIR FSRFISTEQL ADHVNDILDR YPDLEEEVIT ALDHD // ID Y285_MYCGE Reviewed; 347 AA. AC P47527; Q49369; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 64. DE RecName: Full=Uncharacterized protein MG285; GN OrderedLocusNames=MG285; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-164. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71507.1; -; Genomic_DNA. DR EMBL; U02266; AAD12532.1; -; Genomic_DNA. DR PIR; E64231; E64231. DR RefSeq; WP_010869407.1; NZ_AAGX01000018.1. DR STRING; 243273.MgenG_010200003295; -. DR EnsemblBacteria; AAC71507; AAC71507; MG_285. DR KEGG; mge:MG_285; -. DR PATRIC; 20010082; VBIMycGen98045_0328. DR OMA; YEIESAN; -. DR OrthoDB; EOG66TG4V; -. DR BioCyc; MGEN243273:GH2R-319-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 347 Uncharacterized protein MG285. FT /FTId=PRO_0000210512. FT CONFLICT 164 164 E -> R (in Ref. 2; AAD12532). FT {ECO:0000305}. SQ SEQUENCE 347 AA; 40052 MW; F88BD38C2D499EFC CRC64; MAAILNVQRI QNNQVTEYTM SPVRNFANTK DVYFDAQLTN IESKIDSSRA QIHLTIALKY NTNLPDNIFQ AHFSLGNWQS DKIQLQKAPD KKHDSLNSIK YFYAFLDVPR SALAKKEINR FSNVVARVLR ISFRLQDQSE KGNWSDYHLF DTVASELYAT VIKETINFGN MIKINALDGS KQLTSSQGSF KYSWTMYDYR NLEQLDEVRN LINISFDKPV QIVNVDVKIH YVPTKGRLQE IKQQGEFENN LDVNEKLKLN LIGNWNFDKH NKKLISDISG TGIFLPQGGY GSYEIMIGAT VGNDFYTIIA NNQFKYETPL DDLEQNDFFE VNYLPVYSTY NFSDLTQ // ID Y296_MYCGE Reviewed; 129 AA. AC P47538; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 62. DE RecName: Full=Uncharacterized protein MG296; GN OrderedLocusNames=MG296; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71517.1; -; Genomic_DNA. DR PIR; G64232; G64232. DR RefSeq; WP_009885876.1; NZ_AAGX01000008.1. DR ProteinModelPortal; P47538; -. DR SMR; P47538; 1-129. DR EnsemblBacteria; AAC71517; AAC71517; MG_296. DR KEGG; mge:MG_296; -. DR PATRIC; 20010122; VBIMycGen98045_0347. DR OMA; FETFRIN; -. DR OrthoDB; EOG6JX7T2; -. DR BioCyc; MGEN243273:GH2R-332-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 1.20.120.510; -; 1. DR Gene3D; 1.20.890.20; -; 1. DR InterPro; IPR027371; Mg296_homologue_C. DR InterPro; IPR027374; Mg296_homologue_N. DR InterPro; IPR019097; Mg296_protein. DR Pfam; PF09644; Mg296; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 129 Uncharacterized protein MG296. FT /FTId=PRO_0000210520. SQ SEQUENCE 129 AA; 15318 MW; 9336AF153C9C36B6 CRC64; MKPQLIAFKK FLQTEFQAVD FETFRINFNL CLKREQDNIV IYEDDDYDDQ PFFFKPMLSD GFFIQTEVIK QLDYLAKVVE NPKDSDQQCC QNFYEALIVF ISALAITKGI NPNRFHQRLV NRFAIHAVY // ID Y321_MYCGE Reviewed; 934 AA. AC P47563; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Uncharacterized lipoprotein MG321; DE Flags: Precursor; GN OrderedLocusNames=MG321; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71543.1; -; Genomic_DNA. DR PIR; E64235; E64235. DR STRING; 243273.MgenG_010200003028; -. DR EnsemblBacteria; AAC71543; AAC71543; MG_321. DR KEGG; mge:MG_321; -. DR PATRIC; 20010176; VBIMycGen98045_0372. DR OMA; AQLNRFN; -. DR OrthoDB; EOG6SFP68; -. DR BioCyc; MGEN243273:GH2R-359-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 25 934 Uncharacterized lipoprotein MG321. FT /FTId=PRO_0000014034. FT LIPID 25 25 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 25 25 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 934 AA; 103000 MW; EDA036543736C6F1 CRC64; MKLKKRYLLL GSTLTVSAAL ILSACASSQL NKGVFFTSSS ADLLKNNSVP LSMFNVSPTS SFFGNAYAGL TNYVATGTNR DDGVNVTDQI KEKLVLELAL SVTGYKKTTH SGLKGRAQKN GSTDSSDGSS KNDYTKFNEW DAIGTIYRDS SKSITEDPNY HKITQEATRY EFTINTSLSW VDNAGREVKQ NNQPVKLSSK DFERGFETYI LSSNLGFNRN GYFIDLMGLD VEKTVGMDKT NGSSDGNGKG IEITDENYDV ENYRSVDDNK FNVYLTSPFP FFLSMMSKEF FFPIPHTHPK VKALKLGKDS PLKYNQNNNR KILDQANTNF DGIYGGGVNA WKDTWSVGPY YVESFNQAQI VFKRNQIYDA IITPNLPKTR QENEKPIPAI VSYFQPGATP EVFYSSYIAG GLSASAVPYS QQQDARSRFN GTGDLRWLKI QKTAQSAQVT YSGKPYVAND STVQLNANIT ETEAKFLYNS ESEEALTIRA GINGLINWKN LAIIDLPNSG DVNYSTVPFG IFKEKPANGT SSGTNTDGIE NDYYYKINNN QRLGLIPEQT GTFQKDKNVL DTATVKLSYY SSTKTNGAQV RTASTSGSSS QTSQVSSKQV SVTKQSFISA LKKVGFTGNN PLHFNIKLGN ASLSSNQVDY YNALKQALTE LGNDNGENLI IPEIILGDAQ GPTRNEWYIG LSSVLGFSYW SPDYDGVGTW LDAATQLNSE GIGEVITYNS GSHIVRTLLL AASQNNVFNQ IENKLQNNTT TNGKDWCSCI TSADLFKDDP YVIKNFGTNG NNGTSASLAF TKKALSLLKF LVDNKVLKAD KVKEAIKDPD KYLSKRSKID DNKPANVSDI HIGYELKDLY DNAAQLNRFN SIWAEQDTDN AKFLITVVDS YFPVLPVSAP GLNETIPSLL KPWFSLRNAP SGIATMRDSG YIDE // ID Y322_MYCGE Reviewed; 558 AA. AC P47564; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=Uncharacterized cation transporter MG322; GN OrderedLocusNames=MG322; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TrkH potassium transport 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; L43967; AAC71544.1; -; Genomic_DNA. DR PIR; F64235; F64235. DR STRING; 243273.MgenG_010200003038; -. DR EnsemblBacteria; AAC71544; AAC71544; MG_322. DR KEGG; mge:MG_322; -. DR PATRIC; 20010196; VBIMycGen98045_0375. DR eggNOG; ENOG4105CZN; Bacteria. DR eggNOG; COG0168; LUCA. DR OMA; AYMLARP; -. DR OrthoDB; EOG6HTNT6; -. DR BioCyc; MGEN243273:GH2R-367-MONOMER; -. DR Proteomes; UP000000807; 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:0008324; F:cation transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003445; Cat_transpt. DR Pfam; PF02386; TrkH; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Ion transport; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 558 Uncharacterized cation transporter MG322. FT /FTId=PRO_0000070481. FT TRANSMEM 21 41 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 160 180 Helical. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TRANSMEM 251 271 Helical. {ECO:0000255}. FT TRANSMEM 303 323 Helical. {ECO:0000255}. FT TRANSMEM 386 406 Helical. {ECO:0000255}. FT TRANSMEM 413 433 Helical. {ECO:0000255}. FT TRANSMEM 454 474 Helical. {ECO:0000255}. FT TRANSMEM 479 499 Helical. {ECO:0000255}. FT TRANSMEM 519 539 Helical. {ECO:0000255}. SQ SEQUENCE 558 AA; 61612 MW; 71E69CC184EC708D CRC64; MVKLTTWLKK IGWGETITQR IFCFYIYCIL FGSLLLFLPI ALQDNYQKVV SYGIDWQGKR FEQKTDYNFL DALFLSTSAF SDTGLSTVVV SKTYSIFGQI VLAVLLQLGG IGFVVIAFLA WRLFNFHKKE QYSFYEKLML QSERGGSKLG NTSEMILVSI IFLFIVELIY GFLYGILFYF IPGFEPANLF ADHAKVSTQL KALVVDSNQT IAAFNDINKA FQAGFFHSLS AVNNAGIDLI GGSSFVPYRN GLGIIIQWLT ISQIIFGGIG YPCLFDGFEA IKKKIKYGRH TKHQFSLFTK LTVITNIVVI LLFFTLLLMV EFIASDSLTN TIVNFSDEKK SLINTQLQSQ SNQAIHASVF GNNPNASRVM QLFFMVISSR SAGFSVFPVA SEIQTTKIII ALAMFIGASP SSTAGGIRTT TLAVIFLALV AKFKGQKEVK AFKRSIDQTT VIDAFLVLII SLIAVLLTAV LLPLSMEQPV SFIDALFETT SAFGTVGLSS GATVNIALDP NRNTFNFLAL CLLMVMGQVG VSSSVLTFVR KHPKANSYSY PKEAVKIG // ID Y332_MYCGE Reviewed; 239 AA. AC P47574; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 84. DE RecName: Full=Probable transcriptional regulatory protein MG332 {ECO:0000255|HAMAP-Rule:MF_00693}; GN OrderedLocusNames=MG332; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71556.1; -; Genomic_DNA. DR PIR; G64236; G64236. DR RefSeq; WP_009885985.1; NZ_AAGX01000016.1. DR ProteinModelPortal; P47574; -. DR STRING; 243273.MgenG_010200003225; -. DR EnsemblBacteria; AAC71556; AAC71556; MG_332. DR KEGG; mge:MG_332; -. DR PATRIC; 20010220; VBIMycGen98045_0387. DR eggNOG; ENOG4105CDY; Bacteria. DR eggNOG; COG0217; LUCA. DR OMA; MKRWGNM; -. DR OrthoDB; EOG6HJ29R; -. DR BioCyc; MGEN243273:GH2R-380-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 1 239 Probable transcriptional regulatory FT protein MG332. FT /FTId=PRO_0000175845. SQ SEQUENCE 239 AA; 26964 MW; 245612EF66640DB3 CRC64; MPRKHLIANQ TNKKQQTSAK QLQKLAKRIA SAVKKGGTNI QSNPHLKVAV DLALAKGLSM DSIKRNIHGS EKDTTKISEF CYEIFGPNGV GIIVFGLTDN PNRLLSSLNG YLAKLKGQLA KPNSVKINFQ EEGIIFVNKN NYLKDDLIEL LILDNINLID VDYDEECFEI SLHSNSYFHA KELLKKNNFS IVDSEIKLVP LLTVDLDRNQ QTLLSRFLNA CEEDDDIQFV VHNANPWEE // ID Y350A_MYCGE Reviewed; 224 AA. AC Q9ZB72; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 74. DE RecName: Full=Uncharacterized protein MG350.1; GN OrderedLocusNames=MG350.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. 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; L43967; AAC71586.1; -; Genomic_DNA. DR RefSeq; WP_009885808.1; NZ_AAGX01000006.1. DR STRING; 243273.MgenG_010200001888; -. DR EnsemblBacteria; AAC71586; AAC71586; MG_521. DR KEGG; mge:MG_521; -. DR PATRIC; 20010276; VBIMycGen98045_0412. DR eggNOG; ENOG41071SP; Bacteria. DR eggNOG; ENOG410Z0CN; LUCA. DR OMA; LITPLYW; -. DR OrthoDB; EOG60SCM1; -. DR BioCyc; MGEN243273:GH2R-404-MONOMER; -. DR Proteomes; UP000000807; 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 1 224 Uncharacterized protein MG350.1. FT /FTId=PRO_0000210557. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT TRANSMEM 91 111 Helical. {ECO:0000255}. FT TRANSMEM 119 139 Helical. {ECO:0000255}. FT TRANSMEM 142 162 Helical. {ECO:0000255}. FT TRANSMEM 174 194 Helical. {ECO:0000255}. SQ SEQUENCE 224 AA; 26024 MW; 75A16D9C9CB13BF3 CRC64; MNGNKLVFLP KKSYHQLFNI TFSAMMLALA IITSLISEFI SIPFFSQLKL TFDISVVFLV ACAFFVSLGW SLTITLASAL TSFFWNTNNV IGVLTVTLAN LSTILFTRLY FCLFSKRRFC WIFVFLFTTL SNALLLTTLN GILITPLFWY YFGYVQTPNF LIVAEQYNKN TDFHFFFFGI NNYWLGIFCL YSFFNLVKFG LVSCFGVPIM RSFQKFYWKR ALAK // ID Y354_MYCGE Reviewed; 137 AA. AC P47596; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 71. DE RecName: Full=Uncharacterized protein MG354; GN OrderedLocusNames=MG354; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71579.1; -; Genomic_DNA. DR PIR; B64239; B64239. DR RefSeq; WP_009885812.1; NZ_AAGX01000006.1. DR PDB; 1TM9; NMR; -; A=1-137. DR PDBsum; 1TM9; -. DR ProteinModelPortal; P47596; -. DR SMR; P47596; 1-137. DR STRING; 243273.MgenG_010200001908; -. DR EnsemblBacteria; AAC71579; AAC71579; MG_354. DR KEGG; mge:MG_354; -. DR PATRIC; 20010284; VBIMycGen98045_0416. DR OMA; ICSTRES; -. DR OrthoDB; EOG64R67M; -. DR BioCyc; MGEN243273:GH2R-408-MONOMER; -. DR EvolutionaryTrace; P47596; -. DR Proteomes; UP000000807; Chromosome. DR InterPro; IPR015271; DUF1951. DR Pfam; PF09188; DUF1951; 1. DR SUPFAM; SSF110009; SSF110009; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 137 Uncharacterized protein MG354. FT /FTId=PRO_0000210561. FT HELIX 6 15 {ECO:0000244|PDB:1TM9}. FT HELIX 23 31 {ECO:0000244|PDB:1TM9}. FT STRAND 34 42 {ECO:0000244|PDB:1TM9}. FT HELIX 44 51 {ECO:0000244|PDB:1TM9}. FT HELIX 57 74 {ECO:0000244|PDB:1TM9}. FT HELIX 86 89 {ECO:0000244|PDB:1TM9}. FT HELIX 92 106 {ECO:0000244|PDB:1TM9}. FT HELIX 119 129 {ECO:0000244|PDB:1TM9}. FT HELIX 131 134 {ECO:0000244|PDB:1TM9}. SQ SEQUENCE 137 AA; 15704 MW; 0A9A77DCDC10BC9E CRC64; MEQNNIKEQL ISFFNQACST HQERLDFICS TRESDTFSSV DVPLEPIKNI IEITKDENQQ IEITKIAVNN IKTLSSVGAT GQYMASFFST NSEPAIIFCV IYFLYHFGFL KDNNKKQIIK KAYETIADNI ADYLNEN // ID Y360_MYCGE Reviewed; 411 AA. AC Q49426; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Uncharacterized protein MG360; GN OrderedLocusNames=MG360; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 umuC domain. {ECO:0000255|PROSITE- CC ProRule:PRU00216}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71585.1; -; Genomic_DNA. DR PIR; H64239; H64239. DR RefSeq; WP_010869448.1; NC_000908.2. DR ProteinModelPortal; Q49426; -. DR STRING; 243273.MgenG_010200001953; -. DR EnsemblBacteria; AAC71585; AAC71585; MG_360. DR KEGG; mge:MG_360; -. DR PATRIC; 20010300; VBIMycGen98045_0424. DR eggNOG; ENOG4107QKI; Bacteria. DR eggNOG; COG0389; LUCA. DR KO; K02346; -. DR OMA; QMEENDL; -. DR OrthoDB; EOG6FZ4D8; -. DR BioCyc; MGEN243273:GH2R-414-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 3.30.1490.100; -; 1. DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger. DR InterPro; IPR024728; PolY_HhH_motif. DR InterPro; IPR001126; UmuC. DR Pfam; PF00817; IMS; 1. DR Pfam; PF11799; IMS_C; 1. DR Pfam; PF11798; IMS_HHH; 1. DR SUPFAM; SSF100879; SSF100879; 1. DR PROSITE; PS50173; UMUC; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 411 Uncharacterized protein MG360. FT /FTId=PRO_0000173984. FT DOMAIN 20 199 UmuC. {ECO:0000255|PROSITE- FT ProRule:PRU00216}. SQ SEQUENCE 411 AA; 47466 MW; F3FA0C41E9018BAD CRC64; MINTFTYFEP EYLIDKNLIF LYFDFDAFFA SVEELENPEL VNQPLIVGNR FSRSVVSTCN YVARSYGIRS GMSILKALEL CPNAIFAHSN FRNYRKHSKR IFSVIESTFS LKIDVLSVDE GVACFQNISF KKAFLIAKKI KNFVFQNLRI KISIGISDHF LIAKIFSNQA KPFGIKSCSV KDIKKKLWPL PITEIPGIGE KHIDLVFKNN FYKINDLAVC EDASLLKKVF GNFWESLKAV SLGKWYTDNN NQVKSRSFAV SETLEDLNYS NNQLNKKLTQ IFDQLFIRLQ LSSQVCKGIV VQLKSNDFIV NSHSNKMKKY SNDYRKLLSI TKRLFNRLLI NTEKNVRLIG ISFFDLKKID TDEGQKKSLF YQFIPKSISK LSEESSLDKL IFDINESFGF EIIKRANKLK S // ID Y366_MYCGE Reviewed; 667 AA. AC P47606; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 61. DE RecName: Full=Uncharacterized protein MG366; GN OrderedLocusNames=MG366; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71593.1; -; Genomic_DNA. DR PIR; E64240; E64240. DR RefSeq; WP_010869451.1; NC_000908.2. DR EnsemblBacteria; AAC71593; AAC71593; MG_366. DR KEGG; mge:MG_366; -. DR PATRIC; 20010314; VBIMycGen98045_0431. DR OMA; YANLEED; -. DR OrthoDB; EOG6TN42C; -. DR BioCyc; MGEN243273:GH2R-421-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR InterPro; IPR021301; DUF2779. DR Pfam; PF11074; DUF2779; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 667 Uncharacterized protein MG366. FT /FTId=PRO_0000210567. SQ SEQUENCE 667 AA; 78117 MW; 450389698D0690D8 CRC64; MITKSFFLKN FDRSKELIPL SYNDVFSAVN QFLKSYTDVN DIDIIEENLI EDPVFELDVL ELLNEDPMLL LDSKNPRVQE AKIIANKAKK NIKDYFNLPI FFDTDSLDKN VSVYQKAELT EKKIQEIITS KKSAIIFKPI FEIEDCLIQP DAIIVHEKGL CEFVVIKATT NTKRKYFLEI IYDFVLFKKI GKYKLLNYYF CTVKYELQNK NNVSFFLNTE IKTSKNSFSL SSKEKDYFKN KPFNHPEKIA YIHKKKSNGV NGFLIVKLID NLIKNNIVDL NKISDFVTKE IDSKSVRNIQ PLIKNAAKIQ INFWDQIQDI KKYQELKINQ IVFNYSENFD SFWSNYLLRN LIKLVFAHKY NEIFKLSGKL ANWSQLTYAY KENKSITINQ LLHELNQKKS KANFNNSTNK ISFFLEAWNS EKGFAIGNKF KNTWNKLKKK KVYFDFETIS SSIRIINNSL PFSQIVTQCS LIVDKNEIDD KRKLNCENLI FDPLFISVND FKKVIDSLYQ NNCSDYSFVV FNKSFEKNRL LEMATLINEQ IYKEKVKAIV DNLFDLADIF TIENNCLAFK QLNGFSSIKK VLTIIDESFL KASKSIGYQN LKIQKGDVAQ EVALSRFLNC LNKNEWNQVA FELKKYCEND VRAMISIVLF IQDLIKKNDL FTFYSEN // ID Y371_MYCGE Reviewed; 324 AA. AC Q49428; Q49366; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=Uncharacterized protein MG371; GN OrderedLocusNames=MG371; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-229. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Belongs to the mgp1/MG371 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; L43967; AAC71598.1; -; Genomic_DNA. DR EMBL; U02263; AAD12529.1; -; Genomic_DNA. DR PIR; A64241; A64241. DR RefSeq; WP_010869455.1; NC_000908.2. DR ProteinModelPortal; Q49428; -. DR STRING; 243273.MgenG_010200002906; -. DR EnsemblBacteria; AAC71598; AAC71598; MG_371. DR KEGG; mge:MG_371; -. DR PATRIC; 20010324; VBIMycGen98045_0436. DR eggNOG; ENOG4107XI1; Bacteria. DR eggNOG; COG0618; LUCA. DR KO; K06881; -. DR OMA; KKRVDFN; -. DR OrthoDB; EOG6FBX0G; -. DR BioCyc; MGEN243273:GH2R-426-MONOMER; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 324 Uncharacterized protein MG371. FT /FTId=PRO_0000210572. SQ SEQUENCE 324 AA; 37232 MW; F1DEF246DF913270 CRC64; MISIDPQFIK NFSKKVKQFD KFSLFVHVNP DFDAFGSAFA FKTFLNTFFS EKKAYVMGSY NINADGRELF PFEQTDINDD FVKESLAIIF DTSNQERVLT QKHKLAKETV RIDHHPRTEK FADMEWIDSS FSATAEMIGY LILQMGYKLN DEIASYLYAG IITDTQRFWG PTTTPQTFAL TAKLMETGFN RNKVHDAVYL KPLLEHKYFS YVLSKAKITK NGLAYALIKK GAYKHFGVVS PLPMVHALNN IKGVKIWTTV YFNESIKKWI GSIRSRNIPI NNFAQMFNGG GHKYAAAFVL DEKNQFMKLV QIMDDFLAKQ NENS // ID Y443_MYCGE Reviewed; 395 AA. AC P47681; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Uncharacterized protein MG443; GN OrderedLocusNames=MG443; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC72463.1; -; Genomic_DNA. DR PIR; I64248; I64248. DR RefSeq; WP_010869483.1; NC_000908.2. DR EnsemblBacteria; AAC72463; AAC72463; MG_443. DR KEGG; mge:MG_443; -. DR PATRIC; 20010472; VBIMycGen98045_0509. DR OMA; LVDENHN; -. DR OrthoDB; EOG6XDGRN; -. DR BioCyc; MGEN243273:GH2R-496-MONOMER; -. DR Proteomes; UP000000807; 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; IPR019264; DUF2179. DR InterPro; IPR003740; YitT. DR Pfam; PF10035; DUF2179; 1. DR Pfam; PF02588; YitT_membrane; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 395 Uncharacterized protein MG443. FT /FTId=PRO_0000210616. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 67 87 Helical. {ECO:0000255}. FT TRANSMEM 97 117 Helical. {ECO:0000255}. FT TRANSMEM 128 148 Helical. {ECO:0000255}. FT TRANSMEM 196 216 Helical. {ECO:0000255}. FT TRANSMEM 241 261 Helical. {ECO:0000255}. FT TRANSMEM 281 301 Helical. {ECO:0000255}. SQ SEQUENCE 395 AA; 44659 MW; DAF03CCE62686C2E CRC64; MKFFNNLFKK ESKITVASGS KRVRISNSFL MFSNLYEAKK PLKYVLVYLL SIINAFLLLI FIQKTGLYSF GISSLTQGFA RLVFVLLKSF DETQRLLIFN ILYWLLYVFI NIPLIIFSYK KIGKNFTILS THFVVASNVF GFLISIIPGS DNLPPMLASI TDTNFWKAAK DLNQSAGFVP FLWSDTSQGN VIISTFIYAA IYGFYNGISV SLLYILGGSA GGADFLTQYY ARKKNRSVGS ILFYVNSFIL IIAILIGSFV AGSLLLQDVN NYRDSAWEVS LFFSPNLIAT FFSILLTGTV VSYLFPRYNF AEIKVFTDKL EEVRKALLSD NANHSLSIQE TLGGYSLLKK KMIVSVSMYV EIPHLIKIIR QIDKDCLVSI TRIRGIDGHI YLRQN // ID Y447_MYCGE Reviewed; 547 AA. AC P47685; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Uncharacterized protein MG447; GN OrderedLocusNames=MG447; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 107-215. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC72467.1; -; Genomic_DNA. DR EMBL; U01788; AAD10610.1; -; Genomic_DNA. DR PIR; D64249; D64249. DR RefSeq; WP_010869486.1; NC_000908.2. DR EnsemblBacteria; AAC72467; AAC72467; MG_447. DR KEGG; mge:MG_447; -. DR PATRIC; 20010482; VBIMycGen98045_0514. DR OMA; NTIMNTS; -. DR OrthoDB; EOG63NMF0; -. DR BioCyc; MGEN243273:GH2R-500-MONOMER; -. DR Proteomes; UP000000807; 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:0015297; F:antiporter activity; IEA:InterPro. DR GO; GO:0015238; F:drug transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002528; MATE_fam. DR Pfam; PF01554; MatE; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 547 Uncharacterized protein MG447. FT /FTId=PRO_0000210618. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 145 165 Helical. {ECO:0000255}. FT TRANSMEM 203 223 Helical. {ECO:0000255}. FT TRANSMEM 231 251 Helical. {ECO:0000255}. FT TRANSMEM 263 283 Helical. {ECO:0000255}. FT TRANSMEM 298 318 Helical. {ECO:0000255}. FT TRANSMEM 351 371 Helical. {ECO:0000255}. FT TRANSMEM 397 417 Helical. {ECO:0000255}. FT TRANSMEM 432 452 Helical. {ECO:0000255}. FT TRANSMEM 470 490 Helical. {ECO:0000255}. FT TRANSMEM 499 519 Helical. {ECO:0000255}. SQ SEQUENCE 547 AA; 62053 MW; E6D115C419A2E81B CRC64; MNSKRDRFEK QLLIKNVFES KQLFLTILRF TVPTFFFALF SAAYVFIDQI MVIKFVPRSE LNPDSIFTDQ SLIDEFKNSA FYKSDSFLSS GLNIKQFIKT VLNISQPLIV LLNAINIFIP LGTGVIFSKA IGRNDQNKIQ EAWNTGLIST TVFGLITQFL VLSFAKEWLH YNLDQSSFEQ NFQANSFQQF FNKKAIDVAS EYVYILIGLN IIPMLSRLFF YLAQSEGRQL FIAIVPPIAN LINILIVFLL VRYSSLGVIG SAVAGILGYL INFLAYIIYL IYLNKRNLTY LTFKTIKLNK IDFNLLVVVS LIGMASFFRN GSLSIVTTFY ESFLVNLTKA TTDKNDVFYL TLLTGPIAIS NLASAAIFGL LQGVRTVSSY KFGQKKYDEI KKINIYTVII CISFGSLIYL LTAVAFGKQI LSSFFDVSDQ NLDLANYFSL IVQAQVFFVA TGANSQQYFQ NTNRVLYSWI VSLTHGLFVF IPLLFIFQAI TLQTNNIEVF IWLLTANAAL AGLINIAFGQ IHTNLFMDKY FANPPQNKLV KFIEKYS // ID Y467_MYCGE Reviewed; 311 AA. AC P47705; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Putative ABC transporter ATP-binding protein MG467; GN OrderedLocusNames=MG467; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-117. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC72487.1; -; Genomic_DNA. DR EMBL; U01741; AAD10551.1; -; Genomic_DNA. DR PIR; F64251; F64251. DR RefSeq; WP_009885566.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47705; -. DR STRING; 243273.MgenG_010200000080; -. DR EnsemblBacteria; AAC72487; AAC72487; MG_467. DR KEGG; mge:MG_467; -. DR PATRIC; 20010528; VBIMycGen98045_0537. DR eggNOG; ENOG4105D6C; Bacteria. DR eggNOG; COG1136; LUCA. DR OMA; LNKFRRE; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-520-MONOMER; -. DR Proteomes; UP000000807; 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 1 311 Putative ABC transporter ATP-binding FT protein MG467. FT /FTId=PRO_0000093249. FT DOMAIN 84 310 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 122 129 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 311 AA; 35051 MW; 67E811B97C10F68B CRC64; MKKGNKTVWN ECIDILDNVK SPSFSANFDD YFKKSKSKPP KKNKKVLNNI KKAELKLKKK ANKKQKANTL YIPPFAQQAK GIVITINKMW KNVHNDDSKQ EISILSDVSL QIAYGEIVII LGSSGSGKTT LLNLIGGYDS ISLGSCIVAN CPLEKCTSEQ LLTYRKNNLG YVYQRYNLIE LLSAYDNIAI SQNLIPKYQR RLDIEELAEK LDIKEILYKF PYEMSGGQKQ RVAIARAIIK EPKLLLCDEP TGALDSNSAE NIINLLQTIN KTYKQTILMV THDVSLTRIA NRIIKISDGK IVSNQLVRPL V // ID Y149A_MYCGE Reviewed; 137 AA. AC Q9ZB80; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized protein MG149.1; GN OrderedLocusNames=MG149.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. 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; L43967; AAC71392.1; -; Genomic_DNA. DR STRING; 243273.MgenG_010200002129; -. DR EnsemblBacteria; AAC71392; AAC71392; MG_478. DR KEGG; mge:MG_478; -. DR PATRIC; 20009730; VBIMycGen98045_0171. DR OMA; FFWSILS; -. DR OrthoDB; EOG6QRWJT; -. DR BioCyc; MGEN243273:GH2R-158-MONOMER; -. DR Proteomes; UP000000807; 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 1 137 Uncharacterized protein MG149.1. FT /FTId=PRO_0000210446. FT TRANSMEM 37 57 Helical. {ECO:0000255}. FT TRANSMEM 64 84 Helical. {ECO:0000255}. SQ SEQUENCE 137 AA; 16086 MW; A30C016FCBCF4E9C CRC64; MMEQQNPDRL KKDRELIYAI VTAKGIISRF FWSILSFLIT NLIFFFAAFV ALLIYLLASV DNQFAFVFIA AIIFIIFYNI FFLSYLLFIY FKGQKAIENN CKYLLTILDI KSDELLPFSL LGSLRKGYML DEMLLEQ // ID Y211_MYCGE Reviewed; 147 AA. AC P47453; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 63. DE RecName: Full=Uncharacterized protein MG211; GN OrderedLocusNames=MG211; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71430.1; -; Genomic_DNA. DR PIR; C64223; C64223. DR RefSeq; WP_009885750.1; NZ_AAGX01000004.1. DR STRING; 243273.MgenG_010200001417; -. DR EnsemblBacteria; AAC71430; AAC71430; MG_211. DR KEGG; mge:MG_211; -. DR PATRIC; 20009880; VBIMycGen98045_0245. DR OrthoDB; EOG6ZWJKD; -. DR BioCyc; MGEN243273:GH2R-222-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR InterPro; IPR019933; DivIVA_domain. DR TIGRFAMs; TIGR03544; DivI1A_domain; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 147 Uncharacterized protein MG211. FT /FTId=PRO_0000210458. SQ SEQUENCE 147 AA; 17471 MW; 3CC920CCA6A052EE CRC64; MDNKNPQKLI TSELLANHRF NFAKDDKGGY DANEVDAFLD QLTKTLIHYE EMKNNEQELK NAYDKLFSDR DQILSRCAKL EADLNTFYEN GYANKVLINR VQELEDKLEK LPDRYTEKLE RIEKLLKKVI KHWTDGEDIS NFEDEFF // ID Y218A_MYCGE Reviewed; 346 AA. AC Q9ZB78; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 11-MAY-2016, entry version 56. DE RecName: Full=Uncharacterized protein MG218.1; GN OrderedLocusNames=MG218.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71439.1; -; Genomic_DNA. DR RefSeq; WP_010869378.1; NC_000908.2. DR PDB; 4XNG; X-ray; 3.00 A; A/B/C/D=63-204. DR PDBsum; 4XNG; -. DR STRING; 243273.MgenG_010200001477; -. DR EnsemblBacteria; AAC71439; AAC71439; MG_491. DR KEGG; mge:MG_491; -. DR PATRIC; 20009914; VBIMycGen98045_0254. DR OMA; DPIQREI; -. DR OrthoDB; EOG6TR0P3; -. DR BioCyc; MGEN243273:GH2R-239-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 346 Uncharacterized protein MG218.1. FT /FTId=PRO_0000210460. SQ SEQUENCE 346 AA; 39575 MW; 96301EFB824B692E CRC64; MVNNEYQQLN TLVESDDEAD LVIANLVKQL NELKQILVSL DNQEASATAV TDKKEEEYNQ NQSSFHNFSK ETLQKQAKRG FLLLERCSLV GLQQLELEYV NLLGRSFDSY QQKTELLNNL KELVDEHFSD TEKIINTLEK IFDVIGGSEY TPVLNSFFNK LLSDPDPIQR EIGLRQFIIT LRQRFKKLSQ KIDSSLKQIE TEAKIATEQV QNSEVMFGPP DIANDHELNL NWPDSETDAI LSSMENELEA ALLAKHQEEP PLIVTPPSLI KPTVSQPEVE VVTPTNNTNF QPQVDLKPTD LKKQQKKKPL NFITRPVFKS NLPPKLSKDD IVHYAHQLLE KNTHNE // ID Y220_MYCGE Reviewed; 102 AA. AC Q49403; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 67. DE RecName: Full=Uncharacterized protein MG220; GN OrderedLocusNames=MG220; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC 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; L43967; AAC71441.1; -; Genomic_DNA. DR PIR; C64224; C64224. DR EnsemblBacteria; AAC71441; AAC71441; MG_220. DR KEGG; mge:MG_220; -. DR PATRIC; 20009918; VBIMycGen98045_0256. DR OMA; YSYKRRN; -. DR OrthoDB; EOG6TFD10; -. DR BioCyc; MGEN243273:GH2R-241-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 102 Uncharacterized protein MG220. FT /FTId=PRO_0000210463. FT TRANSMEM 21 41 Helical. {ECO:0000255}. SQ SEQUENCE 102 AA; 11304 MW; CC332879E197D1D3 CRC64; MWLIDKRSYM YKLEKAQAKQ VVGGLSFWTF SAGLIMIVNA LTGVAHAVND IFQSTTANAN GSDDDNENKN NSYRSKSNYF NTARFKLGLT PGSSSYSFPV FS // ID Y233_MYCGE Reviewed; 99 AA. AC P47475; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized protein MG233; GN OrderedLocusNames=MG233; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: To B.subtilis YsxB. {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; L43967; AAC71454.1; -; Genomic_DNA. DR EMBL; U02141; AAD12419.1; -; Genomic_DNA. DR PIR; G64225; G64225. DR RefSeq; WP_009885770.1; NZ_AAGX01000005.1. DR ProteinModelPortal; P47475; -. DR STRING; 243273.MgenG_010200001592; -. DR EnsemblBacteria; AAC71454; AAC71454; MG_233. DR KEGG; mge:MG_233; -. DR PATRIC; 20009948; VBIMycGen98045_0270. DR eggNOG; ENOG41087JC; Bacteria. DR eggNOG; COG2868; LUCA. DR OMA; MITITFY; -. DR OrthoDB; EOG64V2GR; -. DR BioCyc; MGEN243273:GH2R-255-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007422; Peptidase_C108. DR Pfam; PF04327; Peptidase_C108; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 99 Uncharacterized protein MG233. FT /FTId=PRO_0000210471. FT TRANSMEM 26 42 Helical. {ECO:0000255}. SQ SEQUENCE 99 AA; 10786 MW; 5B0929DD73646B28 CRC64; MIKINISQNF LVAKGHALFA EKGKDIVCAA ISGIIFGGVA WFEPDKIEFT ENKLVPSIAL KLIDPTPNVA VAFSVITVQL KAIANSYPNH IVINEESYE // ID Y241_MYCGE Reviewed; 620 AA. AC P47483; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 76. DE RecName: Full=Uncharacterized protein MG241; GN OrderedLocusNames=MG241; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71462.1; -; Genomic_DNA. DR PIR; F64226; F64226. DR RefSeq; WP_010869388.1; NC_000908.2. DR EnsemblBacteria; AAC71462; AAC71462; MG_241. DR KEGG; mge:MG_241; -. DR PATRIC; 20009964; VBIMycGen98045_0278. DR OrthoDB; EOG6HMXP6; -. DR BioCyc; MGEN243273:GH2R-263-MONOMER; -. DR Proteomes; UP000000807; 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 1 620 Uncharacterized protein MG241. FT /FTId=PRO_0000210479. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 238 258 Helical. {ECO:0000255}. FT TRANSMEM 546 566 Helical. {ECO:0000255}. FT TRANSMEM 584 604 Helical. {ECO:0000255}. SQ SEQUENCE 620 AA; 72875 MW; 22E9DBBB6ECA402D CRC64; MIQKEMEIYN LFTFQIDLDK KLLFEKSNDQ KNYSKIRTHY FKHKFKNKSA VFLNKNLIKN SLNKVLLNFS DFVSGAGIDT VFNQIIDEDP EVLNYLKQVK KDLSKENNAT SQLTFNVTIN PKNTLANFFE GFNIYLHFNE ENNTVIGSFS LQWHIKKTDL FSETKNIAIN NLIHTFCKNN MHEISFMQII NCFSKTKINK HGEIVLKSCA FKQKWQNVVA EKYPFSTASK DLEKINDFFD ALFVMLLLVC HLNKNLLWLC EKTDFFEWKP SQKTALFKAN DSGAYLARML LFLNDWYNEN QAITTADIEN VNEVEDIGKL VEKYSTNQPQ KLSLNSTVYV LQTKQKQFFL KNDFFFNNNE AKLFFLITMK PNVFGLDDTA IANNLNLKKI SDFFKEIDFN DEDILNDFKQ EQEKLLVRRT FNQLLFMNKN TEILSVVNDK QKSVIHNIVW TITYSKAIML KAFDYSKAFE KNRTSDPSLL RSNLTVINRL RYLSEYFQNA SLKYDLLYTK AKQYMQIDKF INDMIRKVNH EDEIFGKFKE RIYLSLGIIS AVVFGIVEFF NCVWTILTVS QEVVDKSVLD PRNIIFISIG TILVLFLLVT ILVFMTRRLY LFEINKKHKN // ID Y263_MYCGE Reviewed; 291 AA. AC P47505; Q49216; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 84. DE RecName: Full=Putative phosphatase MG263; DE EC=3.1.3.-; GN OrderedLocusNames=MG263; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-276. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof 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; L43967; AAC71485.1; -; Genomic_DNA. DR EMBL; U01764; AAD10580.1; -; Genomic_DNA. DR PIR; A64229; A64229. DR RefSeq; WP_009885894.1; NZ_AAGX01000009.1. DR ProteinModelPortal; P47505; -. DR STRING; 243273.MgenG_010200002594; -. DR EnsemblBacteria; AAC71485; AAC71485; MG_263. DR KEGG; mge:MG_263; -. DR PATRIC; 20010026; VBIMycGen98045_0305. DR eggNOG; ENOG4108CDS; Bacteria. DR eggNOG; COG0561; LUCA. DR KO; K07024; -. DR OrthoDB; EOG6K13W0; -. DR BioCyc; MGEN243273:GH2R-290-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 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. DR PROSITE; PS01229; COF_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 291 Putative phosphatase MG263. FT /FTId=PRO_0000054437. FT REGION 60 61 Phosphate binding. {ECO:0000250}. FT ACT_SITE 11 11 Nucleophile. {ECO:0000250}. FT METAL 11 11 Magnesium. {ECO:0000250}. FT METAL 13 13 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 241 241 Magnesium. {ECO:0000250}. FT BINDING 12 12 Phosphate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 217 217 Phosphate. {ECO:0000250}. FT BINDING 244 244 Phosphate. {ECO:0000250}. FT CONFLICT 170 170 L -> S (in Ref. 2; AAD10580). FT {ECO:0000305}. FT CONFLICT 190 190 I -> R (in Ref. 2; AAD10580). FT {ECO:0000305}. SQ SEQUENCE 291 AA; 33423 MW; 708EFFEC6158F4B4 CRC64; MKNEIKYLYS DLDGTIVSWN PKTEFVYQNK SYKNFHEVSD ATISAFYRLQ QKGIKVGIVT GRDYCRVLWL EKQLRTGLPT ITLDGAIIFY QNEILSQTYL DDRFIEGINN IVKRFPEAAY KLNSGWISYF TKNPSVIFEI DYAFLGYFNP NTKLQKKFID STENWDLNKL KVNQVYFDID TCPLAMQKEI IELISVSDVN AKIYEHSMYI IKNGVSKASA LQSLNQFAIP ITKDNTIVCG DGDNDIEMMQ WAKHSVSLIG SNPKCFALAK YHTDSVDNDG IANWIEKNLL C // ID Y265_MYCGE Reviewed; 278 AA. AC P47507; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=Putative phosphatase MG265; DE EC=3.1.3.-; GN OrderedLocusNames=MG265; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof 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; L43967; AAC71487.1; -; Genomic_DNA. DR PIR; C64229; C64229. DR RefSeq; WP_009885896.1; NZ_AAGX01000009.1. DR ProteinModelPortal; P47507; -. DR STRING; 243273.MgenG_010200002604; -. DR EnsemblBacteria; AAC71487; AAC71487; MG_265. DR KEGG; mge:MG_265; -. DR PATRIC; 20010028; VBIMycGen98045_0306. DR eggNOG; ENOG4108K4B; Bacteria. DR eggNOG; COG0561; LUCA. DR KO; K07024; -. DR OMA; FAFTHEL; -. DR OrthoDB; EOG6K13W0; -. DR BioCyc; MGEN243273:GH2R-292-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 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. DR PROSITE; PS01229; COF_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 278 Putative phosphatase MG265. FT /FTId=PRO_0000054439. FT REGION 43 44 Phosphate binding. {ECO:0000250}. FT ACT_SITE 9 9 Nucleophile. {ECO:0000250}. FT METAL 9 9 Magnesium. {ECO:0000250}. FT METAL 11 11 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 227 227 Magnesium. {ECO:0000250}. FT BINDING 10 10 Phosphate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 204 204 Phosphate. {ECO:0000250}. FT BINDING 230 230 Phosphate. {ECO:0000250}. SQ SEQUENCE 278 AA; 31864 MW; C3B14A638F7BDCF6 CRC64; MELKNIIFDL DGTLLSSNQI PLEQTVEFLK DLQKKGIRIT FASGRSHILI RNTATFITPN LPVISSNGAL VYDFASEKPV HIKPIDNKVI PAIMQMLLEF QETFYFYTDK KVFAFTHELD SAKILSTRSQ IVGIDLIENN YIVNKFEKAL DFDFKQHTIT KILLVTKNRE KVPFLAKQLD QIQDINYVSS MTFALDIMQK DVNKAYGLKV LVDNYNLDPE KTMVFGDADN DVEIFQSVKW PVALVNGTDL AKKNAKFITE YDNNHNGIYF FLKKFLAT // ID Y269A_MYCGE Reviewed; 128 AA. AC Q49329; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 3. DT 13-APR-2016, entry version 52. DE RecName: Full=Uncharacterized protein MG269.1; GN OrderedLocusNames=MG269.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-128. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [4] RP IDENTIFICATION. RA Medigue C., Bocs S.; RL Unpublished observations (MAY-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; L43967; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U02215; AAD12511.1; -; Genomic_DNA. DR RefSeq; WP_009885901.1; NZ_AAGX01000009.1. DR STRING; 243273.MgenG_010200002629; -. DR OMA; ACYSSKI; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 128 Uncharacterized protein MG269.1. FT /FTId=PRO_0000210500. SQ SEQUENCE 128 AA; 15068 MW; CFFDC1433A2BA00F CRC64; MDSFVQKYTN GFKSILNKVE KTDFATIKSE FQYNQANLEW VESKVSDLNN YLLDPNQFSD VVSFKKIANE KLDLFVKNHG NKLPFFLFTS FVLAIFSFVS VYVRHHYDLD FNDPDAIISF FRELAFHE // ID Y286_MYCGE Reviewed; 196 AA. AC P47528; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 69. DE RecName: Full=Uncharacterized protein MG286; GN OrderedLocusNames=MG286; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC 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; L43967; AAC71508.1; -; Genomic_DNA. DR PIR; F64231; F64231. DR RefSeq; WP_010869408.1; NC_000908.2. DR STRING; 243273.MgenG_010200003300; -. DR EnsemblBacteria; AAC71508; AAC71508; MG_286. DR KEGG; mge:MG_286; -. DR PATRIC; 20010084; VBIMycGen98045_0329. DR OMA; SKRKLIC; -. DR OrthoDB; EOG6QRW9S; -. DR BioCyc; MGEN243273:GH2R-320-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 196 Uncharacterized protein MG286. FT /FTId=PRO_0000210514. FT TRANSMEM 11 31 Helical. {ECO:0000255}. SQ SEQUENCE 196 AA; 23300 MW; 304553583342413C CRC64; MIFSISKRKL ICGFLLVILT IGGVLGGVYL VTKNNKDNYQ NESNFNNQEQ ISKIPNFKAI GPETQRILRE RNYPLDDSGY YVYKYGEINR YLRNESELDE LINYRVMVPS LKLHHKRVNF DKAFLESKLR KWIIKAIKQH NYFQHFENEP NLRVQYNMNI PAQKIDVNAV WSYKKDNDAA TGKPIRYWDQ FELKLK // ID Y288_MYCGE Reviewed; 414 AA. AC P47530; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 48. DE RecName: Full=Uncharacterized protein MG288; GN OrderedLocusNames=MG288; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Belongs to the MG032/MG096/MG288 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; L43967; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; H64231; H64231. DR OMA; NNIFPVE; -. DR Proteomes; UP000000807; Chromosome. DR InterPro; IPR004306; MG032/096/288_1. DR InterPro; IPR004319; MG032/096/288_2. DR Pfam; PF03072; DUF237; 1. DR Pfam; PF03086; DUF240; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 414 Uncharacterized protein MG288. FT /FTId=PRO_0000215246. SQ SEQUENCE 414 AA; 48435 MW; 6D7480CE59D8273C CRC64; MDFEVDYEGG NNTVNLQFDL KAQTSNFLNL QELQNSFNGN DLNTQLFWKP LINKLVDKNQ NDLTSIAKTA VSDSLFLSNT NIFNSVLKID EQLDLAKTKF EKEIIEPFKK EREKAKADYE EQQRILAEER RKQEEELKRK EEEAKRLKEQ QEQFNKSFEN AKEFKDYWKN QKKDVTDKTQ LIDALKTSFA ADKNKTFSLL INSFTKATSD YYKNNKKDES ENAKKAFSEK GIQFPRQGLE GLYMSDWLRG KLTSYTDIKL NLTSIKIENK ENNPTIDWKN NGIEFRQHYP YKFKFEIDIK YQGGYKLTGL FSWFAPFSGI PSSWNGEMDV KFIVDGDLDY NLVQNTDYPG SLFQFKDNQL LFTLHVKEQI KVQDGKFMDL LKQQNLHNLD LRNGATKPPV VDLASYLHYL VLNS // ID Y304_MYCGE Reviewed; 253 AA. AC P47546; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Putative ABC transporter ATP-binding protein MG304; GN OrderedLocusNames=MG304; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71526.1; -; Genomic_DNA. DR PIR; F64233; F64233. DR ProteinModelPortal; P47546; -. DR STRING; 243273.MgenG_010200002509; -. DR EnsemblBacteria; AAC71526; AAC71526; MG_304. DR KEGG; mge:MG_304; -. DR PATRIC; 20010138; VBIMycGen98045_0355. DR eggNOG; ENOG4108IJ3; Bacteria. DR eggNOG; COG1122; LUCA. DR KO; K16786; -. DR OMA; VINITHD; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-340-MONOMER; -. DR Proteomes; UP000000807; 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 1 253 Putative ABC transporter ATP-binding FT protein MG304. FT /FTId=PRO_0000093245. FT DOMAIN 1 215 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 19 26 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 253 AA; 28669 MW; 639CDE73450BC7E6 CRC64; MLNQISFNVQ DGCHLAVIGH NGSGKSTLVK LLGGFLKAKK GTIFFNDKEL TSVGFNKIGI LLQDPDVQLL ADTLHQELIF TLENHGVLAS EMDKIINEVL TVVELKDKQF TPLKKLSFGE KQRAVFACLL AVKPQIYLLD EAFSMLDNKI SNKLKKFVFD TIKKQNKIVI NITHDFNDLF LADEIIFLSK GSLIKKFAPE AIYEQLDLFH NHHFNLPFPL LLAHKVAKQI NKKTPSLSFE LNDVVNWICK HLK // ID Y441_MYCGE Reviewed; 136 AA. AC P47679; Q49261; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 70. DE RecName: Full=Uncharacterized protein MG441; GN OrderedLocusNames=MG441; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-106. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC 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; L43967; AAC72461.1; -; Genomic_DNA. DR EMBL; U02128; AAD12405.1; -; Genomic_DNA. DR PIR; G64248; G64248. DR RefSeq; WP_009885592.1; NZ_AAGX01000001.1. DR STRING; 243273.MgenG_010200000255; -. DR EnsemblBacteria; AAC72461; AAC72461; MG_441. DR KEGG; mge:MG_441; -. DR PATRIC; 20010468; VBIMycGen98045_0507. DR OMA; LIANIHF; -. DR OrthoDB; EOG6MH5PP; -. DR BioCyc; MGEN243273:GH2R-494-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 136 Uncharacterized protein MG441. FT /FTId=PRO_0000210612. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT CONFLICT 91 91 I -> V (in Ref. 2; AAD12405). FT {ECO:0000305}. SQ SEQUENCE 136 AA; 16324 MW; 577E967961232EEC CRC64; MSVSFLRSKF SLKASVFAFF VLFLFCLKII LVLFRNFGKR FKHFLFNQTS LYLLVRLFQK TEIVWNLIAN IHFFIKTQIQ NLGIRLSRES ISNETFQAVK LFHVNNLGLQ EQEVINSKLS DYFCFFKYRN LLFVNW // ID Y468A_MYCGE Reviewed; 284 AA. AC Q9ZB70; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 84. DE RecName: Full=Putative ABC transporter ATP-binding protein MG468.1; GN OrderedLocusNames=MG468.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. 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; L43967; AAC72489.1; -; Genomic_DNA. DR RefSeq; WP_010869492.1; NC_000908.2. DR ProteinModelPortal; Q9ZB70; -. DR EnsemblBacteria; AAC72489; AAC72489; MG_526. DR KEGG; mge:MG_526; -. DR PATRIC; 20010532; VBIMycGen98045_0539. DR KO; K02003; -. DR OMA; FDRNAFW; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; MGEN243273:GH2R-522-MONOMER; -. DR Proteomes; UP000000807; 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 1 284 Putative ABC transporter ATP-binding FT protein MG468.1. FT /FTId=PRO_0000093251. FT DOMAIN 53 284 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 89 96 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 284 AA; 32256 MW; A696748EFBA43177 CRC64; MVLKTKENKK FDIYLKSSDF AVSKKASKLI KKLNKKHPKR KSLNSFEAKK YDIYFKEVCK AVTNGINNQL ICNHINLKIL PGEFVVILGK SGSGKTSLLS LISALDRPTS GDSFVCGTNT ICCSDAKLTA LRNKNVGYIF QQYGLLRDLD VDDNIKLALP LKKRFNNNLE ELLERLELKE HRHKKVHKLS GGQQQRVAIA RALIKEPKIL FGDEPTGAVN IDISKKILQF FVEYNRDKGT TIVIVTHNEK IVELAKRVIK IHDGKIIVDY LNQNPKTIEQ INWV // ID Y181_MYCGE Reviewed; 420 AA. AC P47427; Q49299; Q49451; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 84. DE RecName: Full=Uncharacterized protein MG181; GN OrderedLocusNames=MG181; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57 AND 397-420. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CbiQ family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD10563.1; 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; L43967; AAC71400.1; -; Genomic_DNA. DR EMBL; U01750; AAD10563.1; ALT_INIT; Genomic_DNA. DR EMBL; U02176; AAD12459.1; -; Genomic_DNA. DR PIR; A64220; A64220. DR RefSeq; WP_009885866.1; NZ_AAGX01000007.1. DR STRING; 243273.MgenG_010200002309; -. DR EnsemblBacteria; AAC71400; AAC71400; MG_181. DR KEGG; mge:MG_181; -. DR PATRIC; 20009794; VBIMycGen98045_0203. DR eggNOG; ENOG4105EK6; Bacteria. DR eggNOG; COG0619; LUCA. DR KO; K16785; -. DR OMA; WRIVPIN; -. DR OrthoDB; EOG6ZSP8P; -. DR BioCyc; MGEN243273:GH2R-190-MONOMER; -. DR Proteomes; UP000000807; 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; IPR003339; ABC/ECF_trnsptr_transmembrane. DR Pfam; PF02361; CbiQ; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 420 Uncharacterized protein MG181. FT /FTId=PRO_0000210448. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 231 251 Helical. {ECO:0000255}. FT TRANSMEM 276 296 Helical. {ECO:0000255}. FT TRANSMEM 317 337 Helical. {ECO:0000255}. FT TRANSMEM 369 389 Helical. {ECO:0000255}. FT CONFLICT 397 402 LGTPEW -> SRYTRM (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 420 AA; 47558 MW; DB1B037D302B39D9 CRC64; MDNFINGYIP RNSFVHKLHP TTKLVIFLLL VILVFVPIGF VFQSVIFLFV TFVFFIAKLP GRFYSSAIKS ITLLFLLLLF VNWFTFRDPG FYLTSDQLNS LPAIDNSKFS FWNISLFNYQ DNVFSQVFAF NRGNLTNLNQ LDFFYKANNA DSYTKVKGID SLASMLANNG NGLSKDKILS AFLDHNLNLY LARSWGANFA GFVVDFNPTT QLFKLTPFLA NASYVLTLRA VILAFYVTQK ILIMILFATV LTSTSSSVEL AYGIERLLWP LKLIKIPVNV FAMTIAIAIR FVPSLLLESQ RILNAQASRG LDFRNGGFLV KMRSLSSLVV PMVSIAFRNA SELASAMEAR GYHPAKKRSS YRQYKITWID ILALFLVFAW FVVIIFLTIR GAVFLDLGTP EWLLTGKINE QVIRDLKVSG // ID Y210A_MYCGE Reviewed; 219 AA. AC P56723; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 1. DT 13-APR-2016, entry version 57. DE RecName: Full=Uncharacterized protein MG210.1; GN OrderedLocusNames=MG210.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71429.1; -; Genomic_DNA. DR PIR; T09720; T09720. DR RefSeq; WP_009885748.1; NZ_AAGX01000004.1. DR STRING; 243273.MgenG_010200001407; -. DR PRIDE; P56723; -. DR EnsemblBacteria; AAC71429; AAC71429; MG_480. DR KEGG; mge:MG_480; -. DR PATRIC; 20009876; VBIMycGen98045_0243. DR OMA; WQIFLED; -. DR OrthoDB; EOG6GTZJH; -. DR BioCyc; MGEN243273:GH2R-220-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 219 Uncharacterized protein MG210.1. FT /FTId=PRO_0000210456. SQ SEQUENCE 219 AA; 25971 MW; 508A59263797BBA0 CRC64; MGKTKNKSDW QIFLEDYRFY FETDFDWVTY LNNCLNSYPD FDIIKFIKKY GPECEKSFLS WQSKAKSDVY SELTNKIKKQ QFSEQLIYQL VQLDALRTNY LIGSLFSDNK TQRKLLKRSW KNAKKEGYTK QEWLMILVGL PFEKGAYHKQ LYDHSRQEIL DLTEVIKKLY LKTETNNDKL EFAATTSKTT AQLTKTMPLN SSDLDKDLME FSGEKWGDN // ID Y225_MYCGE Reviewed; 489 AA. AC P47467; Q49208; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Uncharacterized protein MG225; GN OrderedLocusNames=MG225; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-286. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.genitalium MG226. {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; L43967; AAC71446.1; -; Genomic_DNA. DR EMBL; U01756; AAD10570.1; -; Genomic_DNA. DR PIR; H64224; H64224. DR RefSeq; WP_010869383.1; NC_000908.2. DR STRING; 243273.MgenG_010200001512; -. DR TCDB; 2.A.3.3.15; the amino acid-polyamine-organocation (apc) family. DR EnsemblBacteria; AAC71446; AAC71446; MG_225. DR KEGG; mge:MG_225; -. DR PATRIC; 20009930; VBIMycGen98045_0261. DR eggNOG; ENOG4107FUA; Bacteria. DR eggNOG; COG0531; LUCA. DR OMA; VFITFFY; -. DR OrthoDB; EOG6F55D5; -. DR BioCyc; MGEN243273:GH2R-247-MONOMER; -. DR Proteomes; UP000000807; 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:0015171; F:amino acid transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002293; AA/rel_permease1. DR PANTHER; PTHR11785; PTHR11785; 1. DR Pfam; PF13520; AA_permease_2; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 489 Uncharacterized protein MG225. FT /FTId=PRO_0000210467. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 36 56 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 127 147 Helical. {ECO:0000255}. FT TRANSMEM 158 178 Helical. {ECO:0000255}. FT TRANSMEM 203 223 Helical. {ECO:0000255}. FT TRANSMEM 241 261 Helical. {ECO:0000255}. FT TRANSMEM 286 306 Helical. {ECO:0000255}. FT TRANSMEM 344 364 Helical. {ECO:0000255}. FT TRANSMEM 380 400 Helical. {ECO:0000255}. FT TRANSMEM 419 439 Helical. {ECO:0000255}. FT TRANSMEM 449 469 Helical. {ECO:0000255}. FT CONFLICT 282 286 IFKKA -> TLEDI (in Ref. 2; AAD10570). FT {ECO:0000305}. SQ SEQUENCE 489 AA; 54766 MW; CAFEEE4E83DDF8A9 CRC64; MGQINRKFSE KQFLLFVVNY IAGFGFIATA ISLFRLGPFS WLIFLLVSLV SLIVTLSFAR LSSIDSQNYG GPYLWAKKAV DKEKIAGRMF SFFTGWNNFI IGPLSAATAP LFILNSFSGI DGIRGNLVNT WILIAIGFSF YVLLAFISTK GTSLNKKLIA LFASVKWIVI LSALIVAIYV IARDGNGYSQ NNNLESGFFG RREISFAQIA TVFITFFYSY AGVEDISVMT PDVKTNNFRK ILIVSFIAVF LFYFIGIIIL NGLQNIAQRG GEANSIGNVA DIFKKAAGLG TLIFYGVGAL FNNVSTRLST IIANSRKILP LAYDNYLPSF FYKQNKKGEF QNAIWFTFGT TLIAMTLLVF IPLVASNFDF DNATEYAASV GSAATLLQYI FVFFIIFKFI YKKEPLYQKK WVKTTEELLF CLGTIVIVLM LLVYLFPVID GFSKWETKHT LTIVLYGVLS LIGLVLFLLQ EYKHKNKQNA NKQTTQTTV // ID Y331_MYCGE Reviewed; 212 AA. AC P47573; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 67. DE RecName: Full=Uncharacterized protein MG331; GN OrderedLocusNames=MG331; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC 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; L43967; AAC71555.1; -; Genomic_DNA. DR PIR; F64236; F64236. DR RefSeq; WP_010869436.1; NC_000908.2. DR STRING; 243273.MgenG_010200003220; -. DR EnsemblBacteria; AAC71555; AAC71555; MG_331. DR KEGG; mge:MG_331; -. DR PATRIC; 20010218; VBIMycGen98045_0386. DR OMA; EANEKQW; -. DR OrthoDB; EOG6X1121; -. DR BioCyc; MGEN243273:GH2R-379-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 212 Uncharacterized protein MG331. FT /FTId=PRO_0000210545. FT TRANSMEM 186 206 Helical. {ECO:0000255}. SQ SEQUENCE 212 AA; 25114 MW; D7B95244A8FC887A CRC64; MGRVEKFRFY RQSFDNNKIV KKALINAQKN TESWKKQLNK INQKILINYH PFSEFNKNPV KHHTEPNKLF KTLQELIVDL KNTDFKLLEE KVDRMWLNAA YNQTSSGYES WISDDKGIEK INHLSKFYEA NEKQWLKKTS NLTSDLKEYN KILTVFSTES FAFKKSIDNI EPNLFNANKA IFKNLVITLI SFMLFSILFF LIFLIVSFVS FV // ID Y335A_MYCGE Reviewed; 73 AA. AC Q49310; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 88. DE RecName: Full=UPF0154 protein MG335.1; GN OrderedLocusNames=MG335.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-73. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0154 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; L43967; AAC71560.1; -; Genomic_DNA. DR EMBL; U02190; AAD12474.1; -; Genomic_DNA. DR RefSeq; WP_009885966.1; NZ_AAGX01000014.1. DR STRING; 243273.MgenG_010200003106; -. DR EnsemblBacteria; AAC71560; AAC71560; MG_516. DR KEGG; mge:MG_516; -. DR PATRIC; 20010228; VBIMycGen98045_0391. DR eggNOG; ENOG410853A; Bacteria. DR eggNOG; COG3763; LUCA. DR KO; K09976; -. DR OMA; KQIRQIM; -. DR OrthoDB; EOG6J753J; -. DR BioCyc; MGEN243273:GH2R-384-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR HAMAP; MF_00363; UPF0154; 1. DR InterPro; IPR005359; UPF0154. DR Pfam; PF03672; UPF0154; 1. DR ProDom; PD048972; UPF0154; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 73 UPF0154 protein MG335.1. FT /FTId=PRO_0000214968. FT TRANSMEM 6 26 Helical. {ECO:0000255}. SQ SEQUENCE 73 AA; 8281 MW; FADBDF79B437768C CRC64; MNDLALALGL GIPLSLLVGM ILGYFISIKI FKKQMRDNPP ITENQIKAMY AKMGRKLSET QVKEIMRSIK NQK // ID Y343_MYCGE Reviewed; 346 AA. AC P47585; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 58. DE RecName: Full=Uncharacterized protein MG343; GN OrderedLocusNames=MG343; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-150. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71568.1; -; Genomic_DNA. DR EMBL; U01811; AAD12345.1; -; Genomic_DNA. DR PIR; I64237; I64237. DR RefSeq; WP_010869442.1; NC_000908.2. DR EnsemblBacteria; AAC71568; AAC71568; MG_343. DR KEGG; mge:MG_343; -. DR PATRIC; 20010252; VBIMycGen98045_0403. DR OMA; NCICLLE; -. DR OrthoDB; EOG60CWQ3; -. DR BioCyc; MGEN243273:GH2R-393-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 346 Uncharacterized protein MG343. FT /FTId=PRO_0000210551. SQ SEQUENCE 346 AA; 40834 MW; 100F6115947AEB56 CRC64; MSHKINDQTL VNEQRLLAYD FFQNSNKVGL LSTLQYLDFV NFLVRSKKVN YLLVNKVSLP IYQKIYFDNF PFLGFDNNLW SAFGLALRNK SQNDTVFAFV EKTKNTDTEI NKFLKILKTF KGLKIVFLLI NSPEEKTTIK LSDSLIKEIK KQKIKHEVYS LRSFQNKFFK LVRKLEKKHK SKNNVMFVEL NGVFGYETNF EKSNIDFSFT SFQDRFTIEK KLKITSHFIL PHKYLLKNLE NIKHPNFEQK NLIWQQTVKD FNQQFLLHYS KLQVFSNSPT KLKVDALIFD LEFHLIVEIM KGFNFDENCI CLLEGNKEQN PNLPTVSLDT KVADIKTYQG CYFLNN // ID Y348_MYCGE Reviewed; 322 AA. AC P47590; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 74. DE RecName: Full=Uncharacterized lipoprotein MG348; DE Flags: Precursor; GN OrderedLocusNames=MG348; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71573.1; -; Genomic_DNA. DR PIR; E64238; E64238. DR RefSeq; WP_009885806.1; NZ_AAGX01000006.1. DR EnsemblBacteria; AAC71573; AAC71573; MG_348. DR KEGG; mge:MG_348; -. DR PATRIC; 20010264; VBIMycGen98045_0408. DR OMA; YSTITDE; -. DR OrthoDB; EOG60SCM0; -. DR BioCyc; MGEN243273:GH2R-399-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 27 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 28 322 Uncharacterized lipoprotein MG348. FT /FTId=PRO_0000014038. FT LIPID 28 28 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 28 28 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 322 AA; 35186 MW; BEB2495F470161B3 CRC64; MKRLFWNLKH KKAWLVLLLG TGMILSSCSN IDQSFFRELS VESVEKNTAY NQLPVNSTTF RNLVFGTRSY NDGNYVVVIA TETDSSQINF LNGSTNQGTS SLSWGGTLGT TIRQVQNRYS TYPNGVKFLI WNDIAPGSVK WNPYARFPVV DRKNELASQE DKDNSNKLRR SDASAVRYRE IVDFIQRTYG GNVANLINQS NVHAQTVGND VTKAIVIAFR KDNLNKIRAN FYGLDNSTNP NAPGSGQGDS TPPASSGEGG GSDGSSGGDS SSGNGQNTTP TSPQSSQPAV QRSQKSYGIK QHAVRVSVDF LNFLDSVYTP LN // ID Y349_MYCGE Reviewed; 404 AA. AC P47591; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 63. DE RecName: Full=Uncharacterized protein MG349; GN OrderedLocusNames=MG349; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71574.1; -; Genomic_DNA. DR PIR; F64238; F64238. DR EnsemblBacteria; AAC71574; AAC71574; MG_349. DR KEGG; mge:MG_349; -. DR PATRIC; 20010270; VBIMycGen98045_0410. DR eggNOG; ENOG4108YAG; Bacteria. DR eggNOG; COG3611; LUCA. DR KO; K03346; -. DR OMA; WLITEAN; -. DR OrthoDB; EOG6RVFTF; -. DR BioCyc; MGEN243273:GH2R-401-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 404 Uncharacterized protein MG349. FT /FTId=PRO_0000210553. SQ SEQUENCE 404 AA; 47775 MW; 37023D6A8F92CAE4 CRC64; MEDSVLYSFY FWTYMQPNYY RVIKKATSFS GLEMISHAYG QIAGVEVVGF YLWLITEANI QAFNSEIRTP ISRLQNAFNP FEIKKNQVSE WIYKTISKLE SLGLVRTFFS PKRSEITFCI IDPLDWKEFK QNKQLKEKLV EAMGKVEYDR NCLAFDQIDN LQFDNALEIS ANFEVNFTAN QSDVWFSFNF EELHKELVKN KLLISLDEKA KTLINGYFEK YKLSLQQITD CIINSSTQEN ELDFQKLEMM FFQIVKNDTA PILETVSNNK DFFYKNEILD ESTKKAITDC HVNFNSEKYL FLLYGKIDES QLQLVRQLRS DYQLLDKVIN LVLDFSFWKN NGMWREKYIL KIAQSIKINN SQNSYEKTLN NFIRALTLNK KHSLNNIKPV EKTISFTEYF EFIK // ID Y353_MYCGE Reviewed; 109 AA. AC P47595; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 76. DE RecName: Full=Uncharacterized protein MG353; GN OrderedLocusNames=MG353; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71578.1; -; Genomic_DNA. DR PIR; A64239; A64239. DR RefSeq; WP_009885811.1; NZ_AAGX01000006.1. DR ProteinModelPortal; P47595; -. DR STRING; 243273.MgenG_010200001903; -. DR EnsemblBacteria; AAC71578; AAC71578; MG_353. DR KEGG; mge:MG_353; -. DR PATRIC; 20010282; VBIMycGen98045_0415. DR eggNOG; COG0776; LUCA. DR KO; K03530; -. DR OMA; IRNARYQ; -. DR OrthoDB; EOG615VS6; -. DR BioCyc; MGEN243273:GH2R-407-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 4.10.520.10; -; 1. DR InterPro; IPR000119; Hist_DNA-bd. DR InterPro; IPR010992; IHF-like_DNA-bd_dom. DR Pfam; PF00216; Bac_DNA_binding; 1. DR SMART; SM00411; BHL; 1. DR SUPFAM; SSF47729; SSF47729; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 109 Uncharacterized protein MG353. FT /FTId=PRO_0000210559. SQ SEQUENCE 109 AA; 12554 MW; A82FA198AA520695 CRC64; MEKTSNTSKP LSRSEINKII AVATGIKEKK IKEIFKYLNT LLLNELVSRS VCILPENLGK LRITIRNARY QKDMQTGEIR HIPPKPLVRY SPSKTIKETA AKVRWKYAD // ID Y369_MYCGE Reviewed; 557 AA. AC P47609; Q49215; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 77. DE RecName: Full=Uncharacterized protein MG369; GN OrderedLocusNames=MG369; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 383-481. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Contains 1 DhaL domain. {ECO:0000255|PROSITE- CC ProRule:PRU00813}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71596.1; -; Genomic_DNA. DR EMBL; U01763; AAD10579.1; -; Genomic_DNA. DR PIR; H64240; H64240. DR RefSeq; WP_010869453.1; NC_000908.2. DR ProteinModelPortal; P47609; -. DR STRING; 243273.MgenG_010200002018; -. DR PRIDE; P47609; -. DR EnsemblBacteria; AAC71596; AAC71596; MG_369. DR KEGG; mge:MG_369; -. DR PATRIC; 20010320; VBIMycGen98045_0434. DR eggNOG; ENOG4105DP4; Bacteria. DR eggNOG; COG1461; LUCA. DR KO; K07030; -. DR OMA; KVKIDNM; -. DR OrthoDB; EOG60PHBN; -. DR BioCyc; MGEN243273:GH2R-424-MONOMER; -. DR Proteomes; UP000000807; 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 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 557 Uncharacterized protein MG369. FT /FTId=PRO_0000210570. FT DOMAIN 7 206 DhaL. {ECO:0000255|PROSITE- FT ProRule:PRU00813}. FT CONFLICT 456 456 T -> S (in Ref. 2; AAD10579). FT {ECO:0000305}. FT CONFLICT 481 481 N -> I (in Ref. 2; AAD10579). FT {ECO:0000305}. SQ SEQUENCE 557 AA; 62665 MW; 8AE874875626206A CRC64; MSSVNLSSFI DMLRLGCNNI AKNYEYINQL NVFPVPDGDT GTNMKVTITE AIKKLENEKS HIKSFSELGK NFTRDLLLFS RGNSGVIFSQ IMKGFFSNII VNKTSNNSEL SIEDVANAFI VAQEVAYKNV SKPVEGTMLT VARLISNEFK SQKNRPKTLE KLFEQAVKVA WQAVKKTPQM LPVLKASGVV DSGAYGFACF LEGMLSYYGG ESNLDDNTLS TIEIKFNKFK EQHANEDEFG YCTEYVLRLG LKINQTVEKQ KFHQKKFESK VNRIANSVVI ASDKDNGFVK VHAHTLKPHL LLEMGLNYGE FEFVKIDNMN LQVNNKNNSP TKRVLKPAIV ATVPTEAFAE RIREDHDINA ILCTDDTGAP SVFSLLEAVK LTNSSNVIFL LHDKNYFLSA NETIKQLKHQ KINADYVITA NPVESIAALT VFNSDLSIHT NVKAMKRFIK EFASATITQA SKSYKENKVM VNKNDFIAVT NKSIIASESQ LTDCFFKTID ILSKKVKKPE FLLAYYGKDI TEQDAKKMQA LVEKKYKLFC EFSPGEQKVF SYIIGIQ // ID Y370_MYCGE Reviewed; 323 AA. AC P47610; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=Uncharacterized RNA pseudouridine synthase MG370; DE EC=5.4.99.-; DE AltName: Full=RNA pseudouridylate synthase; DE AltName: Full=RNA-uridine isomerase; GN OrderedLocusNames=MG370; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-199. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: RNA uridine = RNA pseudouridine. CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00182}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71597.1; -; Genomic_DNA. DR EMBL; U02220; AAA03374.1; -; Genomic_DNA. DR PIR; I64240; I64240. DR RefSeq; WP_010869454.1; NC_000908.2. DR ProteinModelPortal; P47610; -. DR STRING; 243273.MgenG_010200002901; -. DR EnsemblBacteria; AAC71597; AAC71597; MG_370. DR KEGG; mge:MG_370; -. DR PATRIC; 20010322; VBIMycGen98045_0435. DR eggNOG; COG0564; LUCA. DR KO; K06179; -. DR OMA; HEDAHIM; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; MGEN243273:GH2R-425-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. 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 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; Isomerase; Reference proteome; RNA-binding. FT CHAIN 1 323 Uncharacterized RNA pseudouridine FT synthase MG370. FT /FTId=PRO_0000162741. FT DOMAIN 16 95 S4 RNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00182}. FT ACT_SITE 148 148 {ECO:0000250}. SQ SEQUENCE 323 AA; 37948 MW; 0A0897B8C7367FB8 CRC64; MRIANKFLVP KESENQRIDQ FCLKILPLIK RSDFFKYLRL GKVLLNKTKP QVNTRLKTKD EIAFLFDINP YLQTNNDYLS LDLVKDKLKI IFEDENIIVV DKPTGIVCQP DKKHSIINLS NMLLKHCGYR QFDSNKLNFY PQFAHRIDRN TSGIVIGAKT NKALKELNKV FKNNHLTKRY KGLVFGQFNH LGLQTAYWKK DNNNGIVTVK WKPFPEAKKI STFFENSSYI AQKDMSLITI RLISGRTHQI RACLNLFSNQ LVGDKKYSLI QFKNRNNKYK HQALHAYELV FPKLETSKFP ILTNYSLMQF KSKIVPWFEY LIQ // ID Y374_MYCGE Reviewed; 274 AA. AC P47614; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 69. DE RecName: Full=Uncharacterized protein MG374; GN OrderedLocusNames=MG374; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71601.1; -; Genomic_DNA. DR PIR; D64241; D64241. DR RefSeq; WP_010869456.1; NZ_AAGX01000012.1. DR ProteinModelPortal; P47614; -. DR EnsemblBacteria; AAC71601; AAC71601; MG_374. DR KEGG; mge:MG_374; -. DR PATRIC; 20010330; VBIMycGen98045_0439. DR OMA; KEWINSS; -. DR OrthoDB; EOG67X1T2; -. DR BioCyc; MGEN243273:GH2R-429-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR InterPro; IPR023214; HAD-like_dom. DR Pfam; PF08282; Hydrolase_3; 1. DR SUPFAM; SSF56784; SSF56784; 2. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 274 Uncharacterized protein MG374. FT /FTId=PRO_0000210576. FT NP_BIND 104 111 ATP. {ECO:0000255}. SQ SEQUENCE 274 AA; 31837 MW; 12058F35FA21AE22 CRC64; MDRKIVVLDI NTANFFNTTK DLEVWKNFFN FIQANNHQLV FMSSCWQQAV LYLLDLLSLD DVDIIAESGA IIWISKTNEF IYQSFLDSVS IDTIVHHAII TNSGVFAIGK SKISEEPNTT INYFISLEKY KQFKLIWLTE FDQTLKYQNF LKNLSEMDVS SIYVFSPQYH LDFQLMEHIS SGQPKFHYSN FYNENFLFTS TKNSKFSALE TYVKSKNCSL KDVHYLNVTE VPINNINQLA SVVFLSKKQP DNDEEFNNPE ISIVLKGICE QLMK // ID Y377_MYCGE Reviewed; 193 AA. AC P47617; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 66. DE RecName: Full=Uncharacterized protein MG377; GN OrderedLocusNames=MG377; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71604.1; -; Genomic_DNA. DR PIR; G64241; G64241. DR RefSeq; WP_009885940.1; NZ_AAGX01000012.1. DR ProteinModelPortal; P47617; -. DR SMR; P47617; 4-190. DR STRING; 243273.MgenG_010200002936; -. DR EnsemblBacteria; AAC71604; AAC71604; MG_377. DR KEGG; mge:MG_377; -. DR PATRIC; 20010336; VBIMycGen98045_0442. DR eggNOG; ENOG4106XIK; Bacteria. DR eggNOG; ENOG410YSWE; LUCA. DR OMA; YHELTHI; -. DR OrthoDB; EOG6F55F3; -. DR BioCyc; MGEN243273:GH2R-432-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR InterPro; IPR027304; Trigger_fact/SurA_dom. DR SUPFAM; SSF109998; SSF109998; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 193 Uncharacterized protein MG377. FT /FTId=PRO_0000210580. SQ SEQUENCE 193 AA; 22649 MW; A85E543E6BD281DF CRC64; MATNLKSIAK LQKPIQYDKV IEVDRIFADP AFIEQHRQRI LASFKDAKES ALYHELTHIV IKDNLFSAAM NEIVSYFEFQ INPEELKNVV EGLKRDVVKD ADEKTIQSIA EKIIKKALVF NFLQKEWKVE VSDDIVKRVI SLYYEKTNQN VREYLDDKQK FEGIRTALIE ERMVLETINH FKFHFNLTGQ LPS // ID Y381_MYCGE Reviewed; 218 AA. AC P47621; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 56. DE RecName: Full=Uncharacterized protein MG381; GN OrderedLocusNames=MG381; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71608.1; -; Genomic_DNA. DR PIR; B64242; B64242. DR RefSeq; WP_010869459.1; NC_000908.2. DR EnsemblBacteria; AAC71608; AAC71608; MG_381. DR KEGG; mge:MG_381; -. DR PATRIC; 20010344; VBIMycGen98045_0446. DR OMA; VQHHKKL; -. DR OrthoDB; EOG6D5G9X; -. DR BioCyc; MGEN243273:GH2R-436-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 218 Uncharacterized protein MG381. FT /FTId=PRO_0000210582. SQ SEQUENCE 218 AA; 25500 MW; 2623C57B77CF639D CRC64; MIKLGWASFS NTEFAQDIFI KFANQFYKQD DAGTILFELK KTLGVNQLDE IEKNKKVIIV NQFQNSLGKF LLFNKENTKR INSLANEHIS SFLKKIFRLS GFKDMLIDVQ HHKKLQKCLL REIHLLVCLI NSNQFSDELM QIIEWYQYLK KHSSKLFVIT ASSDKKPVIE PTINEYKAIF GEYLSSFHLD LKNNQSNDLF QKLLDQIKIK ATSKTSLR // ID Y385_MYCGE Reviewed; 236 AA. AC P47625; Q49354; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 75. DE RecName: Full=Uncharacterized protein MG385; GN OrderedLocusNames=MG385; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-78 AND 87-176. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Contains 1 GP-PDE domain. {ECO:0000305}. CC -!- SIMILARITY: To glycerophosphoryl diester phosphodiesterases CC (EC 3.1.4.46). {ECO:0000305}. CC -!- SIMILARITY: To M.genitalium MG293. {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; L43967; AAC71612.1; -; Genomic_DNA. DR EMBL; U02112; AAD12385.1; -; Genomic_DNA. DR EMBL; U02246; AAA03402.1; -; Genomic_DNA. DR PIR; F64242; F64242. DR RefSeq; WP_009885949.1; NZ_AAGX01000012.1. DR ProteinModelPortal; P47625; -. DR STRING; 243273.MgenG_010200003001; -. DR EnsemblBacteria; AAC71612; AAC71612; MG_385. DR KEGG; mge:MG_385; -. DR PATRIC; 20010356; VBIMycGen98045_0451. DR eggNOG; ENOG4105ERW; Bacteria. DR eggNOG; COG0584; LUCA. DR KO; K01126; -. DR OMA; YQFYEND; -. DR OrthoDB; EOG6N0HGM; -. DR BioCyc; MGEN243273:GH2R-442-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:InterPro. 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 PANTHER; PTHR23344; PTHR23344; 1. DR Pfam; PF03009; GDPD; 1. DR SUPFAM; SSF51695; SSF51695; 1. DR PROSITE; PS51704; GP_PDE; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 236 Uncharacterized protein MG385. FT /FTId=PRO_0000210586. FT DOMAIN 4 236 GP-PDE. FT CONFLICT 87 87 S -> M (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 236 AA; 27734 MW; D7A3AF4E3630BDE2 CRC64; MRKQFLIAYR GYSSIAPENT KLAFQAAQVF DFDGIWIDIQ LTKDKQIVVT HKENFKVSNK NLNLNQINLV DLKKVNLASE FKLKVTSQQI QTLKEVLTQF IQPFKYLLIH IKDDKENNNS LLEQLNLLCK DFVLAKEKMI LLSSNFHIIK LINETFKGFK TGFVIANKKA LLVASRDELM RYCRFLVPNE SFYHKNCKEI QNLGLPVILW VIKGLLRYQF YENDRFVKFQ ITAQIY // ID Y397_MYCGE Reviewed; 566 AA. AC P47637; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 71. DE RecName: Full=Uncharacterized protein MG397; GN OrderedLocusNames=MG397; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC 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; L43967; AAC71625.1; -; Genomic_DNA. DR PIR; I64243; I64243. DR RefSeq; WP_010869466.1; NC_000908.2. DR EnsemblBacteria; AAC71625; AAC71625; MG_397. DR KEGG; mge:MG_397; -. DR PATRIC; 20010382; VBIMycGen98045_0464. DR KO; K07158; -. DR OMA; YDSLFYL; -. DR OrthoDB; EOG66TG3D; -. DR BioCyc; MGEN243273:GH2R-454-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005940; C:septin ring; IEA:InterPro. DR GO; GO:0000921; P:septin ring assembly; IEA:InterPro. DR InterPro; IPR010379; EzrA. DR Pfam; PF06160; EzrA; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 566 Uncharacterized protein MG397. FT /FTId=PRO_0000210592. FT TRANSMEM 2 22 Helical. {ECO:0000255}. SQ SEQUENCE 566 AA; 67223 MW; FDD131D23E8EF145 CRC64; MLVFLILLPF LLLVIFGAYL LVCLFVRQNN LLLKKTKQLY NNLKLSNFNC VISPFQLLRN EKQALEQSIK VLKQFQIKFD NEINSAFEQL TVYSKPNNIY RFIWFNRNIK LLNKNLQHLY TKQQEYINLT KNAIVYFNNS YDCLVFYRQA FCFLNQFINN FLIEKYDSLF YLNVLNRISL LFKEIENCIQ AKDVEKQIAF LNKLHNILSQ TIITANRQYM FDIKLSYLTH HFKVLIQKVK QMELMKNKVI NSQDLLKLHE LINNITIKLK DCTNFLNNLN LMLCERNMDE VQEAISWLFQ AVSSKEKSIN LVVENIDDFR NQIQQYEKKN ELLKTTIKAI ELVFQNETDV HDLIIELNEN CDLITKNINN LNHQSLAQNQ INYEKLFYLM SQTNQALEKL KNSLTDLLNL AVNKFDDYRF FVYTLDDFRF KFFQIENLIS DQDLKVPAKT LQVINKSKLE LDNIFTEANN NYLGTFNLFS EKIDLLQIQL TEVICDVVSL VNLRLMCKQA FLFANKYRQK SSHIDRSLEQ LTKLYNRQNY PDTLEGLINL LTKIKTNTKQ DYLELN // ID Y428_MYCGE Reviewed; 171 AA. AC P47667; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=Uncharacterized protein MG428; GN OrderedLocusNames=MG428; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC72449.1; -; Genomic_DNA. DR PIR; C64247; C64247. DR RefSeq; WP_009885604.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47667; -. DR STRING; 243273.MgenG_010200000325; -. DR EnsemblBacteria; AAC72449; AAC72449; MG_428. DR KEGG; mge:MG_428; -. DR PATRIC; 20010442; VBIMycGen98045_0494. DR OMA; DEFRTEI; -. DR OrthoDB; EOG6HB9QP; -. DR BioCyc; MGEN243273:GH2R-482-MONOMER; -. DR Proteomes; UP000000807; 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 Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR000792; Tscrpt_reg_LuxR_C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00196; GerE; 1. DR SUPFAM; SSF88659; SSF88659; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 171 Uncharacterized protein MG428. FT /FTId=PRO_0000210608. SQ SEQUENCE 171 AA; 20259 MW; 87FB346C334E5E72 CRC64; MKNNISDVKL GLLAAKIYWK SWRFLELTED DIISIALHAE QDSKKRFNPE FGLSFDNYLK LNGANFIRSS FRSMVNKVEL LDSKSKYSLE KQNTVLNTPE NYLRSLEFKE IITKAFNKAK NDQERKVFSL YVKGYKNFEI AKKLNISPRR VRYLLDLFKS YIKLLTERYG Y // ID Y432_MYCGE Reviewed; 398 AA. AC Q49432; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=Uncharacterized protein MG432; GN OrderedLocusNames=MG432; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC72453.1; -; Genomic_DNA. DR PIR; G64247; G64247. DR RefSeq; WP_009885601.1; NZ_AAGX01000001.1. DR STRING; 243273.MgenG_010200000300; -. DR EnsemblBacteria; AAC72453; AAC72453; MG_432. DR KEGG; mge:MG_432; -. DR PATRIC; 20010450; VBIMycGen98045_0498. DR eggNOG; ENOG4108ME6; Bacteria. DR eggNOG; COG1284; LUCA. DR OMA; IHIACLL; -. DR OrthoDB; EOG6TR0BM; -. DR BioCyc; MGEN243273:GH2R-486-MONOMER; -. DR Proteomes; UP000000807; 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; IPR019264; DUF2179. DR InterPro; IPR003740; YitT. DR Pfam; PF10035; DUF2179; 1. DR Pfam; PF02588; YitT_membrane; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 398 Uncharacterized protein MG432. FT /FTId=PRO_0000210610. FT TRANSMEM 37 57 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TRANSMEM 122 142 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT TRANSMEM 268 288 Helical. {ECO:0000255}. SQ SEQUENCE 398 AA; 45719 MW; 1E6D92D50F5F0366 CRC64; MKDKNIKISG NFVRIHLSGS FLKFQSIYNL KKLYLQLVIL TIVAFFWGLL GVIFVQFSGL YDIGMASISQ GLARLVNFFI TSQNINVDSA TIFNAIFWLT QILFNVPFFI FGWFKISKKF TLLTLYFVAV SNLFGFFFSY IPGIDNFFLF ANLTTAKDGG FENLINEKGV QLIFWEKSAE KQVSLLFYGL IWGFLQAVFY SVILIIDAST GGLDFLAFWY SEKKYKDIGG ILMLINTVSF IIGYVIGTYL TGSLSVQSYV GDDKHQPFGV AFFLSPNLVF TLLMNIVLGL FTSFYFPKYQ FVKVEVYGKH IEKIRNYLLD NQQWFSITMF EAEGGYSRQK TQVLVTNCLL IKAAKLLEDV RKFDRDALFS ITFIKKLDGY IYDRRTNKQT KHGTENKS // ID Y461_MYCGE Reviewed; 425 AA. AC P47699; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 71. DE RecName: Full=Uncharacterized protein MG461; GN OrderedLocusNames=MG461; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Contains 1 HD 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; L43967; AAC72481.1; -; Genomic_DNA. DR PIR; I64250; I64250. DR ProteinModelPortal; P47699; -. DR EnsemblBacteria; AAC72481; AAC72481; MG_461. DR KEGG; mge:MG_461; -. DR PATRIC; 20010516; VBIMycGen98045_0531. DR KO; K06885; -. DR OrthoDB; EOG6WX4K7; -. DR BioCyc; MGEN243273:GH2R-514-MONOMER; -. DR Proteomes; UP000000807; 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; Reference proteome. FT CHAIN 1 425 Uncharacterized protein MG461. FT /FTId=PRO_0000210629. FT DOMAIN 55 184 HD. SQ SEQUENCE 425 AA; 50365 MW; 87E5CD5A34017E13 CRC64; MQQTFFKDPI LGEIIFDENT KWMYELVNTK AFQRLRNIKQ LGINFHFYPS GVHTRYAHSL GVYELIRRIL NSSAFLNIDQ IKKQTVLVAG LLHDLGHGPH SHAFEIYFAK NPDFKKQLFI HEKVTSMLVN SEPIVSILKA NKIDPNLIGA LIDENQNIQP INWWMRQLIS SDLDTDRMDY LLRDAYFTGT SHSLVDYQSI INGMECVDNQ GTYKIVFQEK CLPFIENFLI TRHHMYQSIY SDGRSIATEL NLWFVFQRIK ALIEEDNFNF HNFKNVESVI KPLLKNQLFK KSLLTCFVKL DDYVFHSFLV NTFETTKDAI LKTLLDSYLN TLKFQVKFYE SCEKRDLDFE LKVKEYQTPS YFITKFNNQF KGFYEGWNKH KNELKIKTSQ NKIKNLSEIS MLVKRSNELF FENSFYRWAN VFYQN // ID Y219_MYCGE Reviewed; 148 AA. AC P47461; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 52. DE RecName: Full=Uncharacterized protein MG219; GN OrderedLocusNames=MG219; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71440.1; -; Genomic_DNA. DR PIR; B64224; B64224. DR RefSeq; WP_010869379.1; NC_000908.2. DR STRING; 243273.MgenG_010200001477; -. DR EnsemblBacteria; AAC71440; AAC71440; MG_219. DR KEGG; mge:MG_219; -. DR PATRIC; 20009916; VBIMycGen98045_0255. DR BioCyc; MGEN243273:GH2R-240-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 148 Uncharacterized protein MG219. FT /FTId=PRO_0000210462. SQ SEQUENCE 148 AA; 16617 MW; BA07AA8FB2D5124A CRC64; MRTSYLKKIP IMNSDSDLKL QKVWIERHVD QDELSLTTTA VELKKSDEQK PVAIKSSDFI GHEELISVPV LLIPTPVVKE IDQPAVIPPV KAKPKATKKK TPVKSKPTSK STKQTKPKQS KPKSKQVQQT KAKPTQIQTK KSNKKTRS // ID Y255A_MYCGE Reviewed; 119 AA. AC Q9ZB77; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 43. DE RecName: Full=Uncharacterized protein MG255.1; GN OrderedLocusNames=MG255.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71480.1; -; Genomic_DNA. DR EnsemblBacteria; AAC71480; AAC71480; MG_494. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 119 Uncharacterized protein MG255.1. FT /FTId=PRO_0000210490. SQ SEQUENCE 119 AA; 13904 MW; 84E67487300F8D86 CRC64; MQFFQENSLV LKPELFSLQK YTKDVYGLNV INQLNLNKHP MLIPLTWDKK QKFISFIESC VQKYSQVKKD NQVFSLTVGK RVFFLLLINK QFKQIKLETA LKYLGFKTSL GAMDSTTES // ID Y256_MYCGE Reviewed; 256 AA. AC P47498; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized protein MG256; GN OrderedLocusNames=MG256; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71476.1; -; Genomic_DNA. DR PIR; C64228; C64228. DR RefSeq; WP_010869397.1; NC_000908.2. DR EnsemblBacteria; AAC71476; AAC71476; MG_256. DR KEGG; mge:MG_256; -. DR PATRIC; 20010000; VBIMycGen98045_0293. DR OMA; SIDSEYF; -. DR OrthoDB; EOG62K24R; -. DR BioCyc; MGEN243273:GH2R-281-MONOMER; -. DR Proteomes; UP000000807; 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 1 256 Uncharacterized protein MG256. FT /FTId=PRO_0000210492. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 73 93 Helical. {ECO:0000255}. FT TRANSMEM 108 128 Helical. {ECO:0000255}. SQ SEQUENCE 256 AA; 30416 MW; D27B8C76D42BB569 CRC64; MHFNSNFKEC FNKIAKKVNS LDSEYYEFSS FIERIRTTFG LLIALTVLSN LIIISFVLIW FFTDGFGQLR LLFFTLFIPF FISLLVAIFL IFLNNSFRNF FQINEKNWLF LWTCVFSSLP IFNLWLIVRL NKTIKNFASD YGFKIVNKYN SLTSGIFVFD FADYVSFEAN LTNWKNTNDK NRNFVNFFET ISKEKTGVVQ KPVLNFQRLY VNRLYYQSKL SVGSNQQTPQ TAFDNLRNYV ENKQRETVRV KQYILT // ID Y259_MYCGE Reviewed; 456 AA. AC Q49404; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=Uncharacterized protein MG259; GN OrderedLocusNames=MG259; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Contains 1 YrdC-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00518}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71479.1; -; Genomic_DNA. DR PIR; F64228; F64228. DR RefSeq; WP_009885794.1; NZ_AAGX01000005.1. DR ProteinModelPortal; Q49404; -. DR STRING; 243273.MgenG_010200001782; -. DR EnsemblBacteria; AAC71479; AAC71479; MG_259. DR KEGG; mge:MG_259; -. DR PATRIC; 20010006; VBIMycGen98045_0296. DR eggNOG; ENOG410819C; Bacteria. DR eggNOG; COG0009; LUCA. DR eggNOG; COG2890; LUCA. DR KO; K07566; -. DR OMA; FCTSANI; -. DR OrthoDB; EOG68Q0SZ; -. DR BioCyc; MGEN243273:GH2R-284-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR Gene3D; 3.90.870.10; -; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR InterPro; IPR006070; YrdC-like_dom. DR Pfam; PF05175; MTS; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR PROSITE; PS00092; N6_MTASE; 1. DR PROSITE; PS51163; YRDC; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 456 Uncharacterized protein MG259. FT /FTId=PRO_0000202026. FT DOMAIN 277 440 YrdC-like. {ECO:0000255|PROSITE- FT ProRule:PRU00518}. SQ SEQUENCE 456 AA; 52808 MW; E8893DCB52A86549 CRC64; MTLYEFFLNQ KLVYQSSPHF NGVFLTILEH YGFQFKTIDK LWKSKLLITS ELTDKIKQQL KCYFIEKIPL PYLLGTIQLR KLTFKTKKGV FIPRIDSLAL IASVNLKKIK TALDLCCGSG TLAIALKKKC DTLDVYGSDI DIQALKLAQQ NALINNVSIN WIEADWFDCF NKIKTPIDLI VTNPPYLKKT QLNKTLNYEP KHSLVFQNKN SYFAYKQLFN LLLTKRSIKQ LIFECSLFQK ERLLNLFSIF KSRPIFNFQK QFIGMKVDNQ KLPVVDIKNT KTIKQLLKMG LAGIVNTDTQ MGLISYSEST LDKIKQRALN KHYVSMFGLE ELKKLPKKLQ QIASYFWPGS YTFIKNNKSY RVPKNLGLLN LFNAIGRVFC TSANISNQKP YTKLSDYQND SYWIKQPCFI IRSTSKVQSN NTPSLVYNLD TKQLVRTTAK QTKQFHKLIT KHQLAI // ID Y260_MYCGE Reviewed; 765 AA. AC P47502; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=Uncharacterized lipoprotein MG260; DE Flags: Precursor; GN OrderedLocusNames=MG260; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG185/MG260 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; L43967; AAC71481.1; -; Genomic_DNA. DR PIR; G64228; G64228. DR RefSeq; WP_009885795.1; NZ_AAGX01000005.1. DR STRING; 243273.MgenG_010200001787; -. DR EnsemblBacteria; AAC71481; AAC71481; MG_260. DR KEGG; mge:MG_260; -. DR PATRIC; 20010008; VBIMycGen98045_0297. DR eggNOG; ENOG4106J71; Bacteria. DR eggNOG; ENOG410Y9FZ; LUCA. DR OMA; GNINIPA; -. DR OrthoDB; EOG6JMMQZ; -. DR BioCyc; MGEN243273:GH2R-285-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004890; Lipoprotein_10_C. DR InterPro; IPR004984; Mycoplasma_lipoprotein_cen_dom. DR Pfam; PF03202; Lipoprotein_10; 1. DR Pfam; PF03305; Lipoprotein_X; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 765 Uncharacterized lipoprotein MG260. FT /FTId=PRO_0000018724. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 765 AA; 84373 MW; 98D639860D949593 CRC64; MKLKGFLAVG VSVFGFSGLL MACSVVSQFD QVDDGKIKLA SSLTSKRAAE ALETVVKKYN DTKDPGDYPI EIVQIAGGYD GGKKDVQTKV STKDKNNFYN LILNYPEIVS TLSRSKMALN FDGVNVDKLH PNFLSFNSRI GGIRDDGIYA IPISMSTDLM VINGPVLHYI LNSARKEGTP TSTTVQATVS SRSAEKKGTL EIANDSETTK LWQNIQTTAQ NNSNETTKEQ KQVKRSSSSS STTSTTGETK DTTKSDNKIK EFWGEYQEVD GGLKNFTFKA SIFENWNETL DFATRIANSF PEKVKNITNK TGLDLQGVLG VDSSSNALYA AVFAAGQANY DNFFFNIDKR TGYADYSNFL NKDSSYQNLE SVYNDFYKLI QANGLFVNRG GSYSSNFEKF HQLAFSVSSS GGYSYYFAKD NAKRLKFSNY AIEYPSFTQT IQAPNSSETE SNLLGTFKLS EKDINLYKGS IPSGKQQGVD AILISNPNLI NILEQAKQKN TAQGSESTTN KIIGYTTTAN VNVDNQNIFS VSKLNNEQFQ RKIIVNATEE TLDQSQTLQS NESIVLPMPG KYKSTDKNKV MITQGPNLIG IHANEKENIE TKKFVNWFLN QSITDWNSNN QQKNSDQTTK TAAEYFTDQA SYILPLKEKF NKSSDLELKG SSSSSNLTTS SASASLLISN NSSTASSPAP KKTNNNSNTF TAKALELFQQ AANNEIIPFS DPSDFRNGTF RNNISSSFNA AVNSKVSFNQ FVQNFINSLG SGFRR // ID Y267_MYCGE Reviewed; 115 AA. AC P47509; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 73. DE RecName: Full=Uncharacterized protein MG267; GN OrderedLocusNames=MG267; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71489.1; -; Genomic_DNA. DR PIR; E64229; E64229. DR RefSeq; WP_009885898.1; NZ_AAGX01000009.1. DR STRING; 243273.MgenG_010200002614; -. DR EnsemblBacteria; AAC71489; AAC71489; MG_267. DR KEGG; mge:MG_267; -. DR PATRIC; 20010032; VBIMycGen98045_0308. DR OMA; FPNINSW; -. DR OrthoDB; EOG69PQCW; -. DR BioCyc; MGEN243273:GH2R-294-MONOMER; -. DR Proteomes; UP000000807; 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 1 115 Uncharacterized protein MG267. FT /FTId=PRO_0000210494. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 47 67 Helical. {ECO:0000255}. FT TRANSMEM 77 97 Helical. {ECO:0000255}. SQ SEQUENCE 115 AA; 13061 MW; 3FC91DA25540421A CRC64; MTLLFKLVKI AILVFLMVIG FFIFIGSFWL NTYQTAQWAD LLASSDASGI ILTIFPNINS WFNATVANQP VLFKTMVHFF IPVGFGLLFG LIIAIIVDIL YRLTKYAIKR SYQSN // ID Y279_MYCGE Reviewed; 218 AA. AC P47521; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 75. DE RecName: Full=Uncharacterized protein MG279; GN OrderedLocusNames=MG279; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC71501.1; -; Genomic_DNA. DR PIR; H64230; H64230. DR RefSeq; WP_010869404.1; NC_000908.2. DR EnsemblBacteria; AAC71501; AAC71501; MG_279. DR KEGG; mge:MG_279; -. DR PATRIC; 20010058; VBIMycGen98045_0321. DR OMA; REPINNY; -. DR OrthoDB; EOG69SKHS; -. DR BioCyc; MGEN243273:GH2R-308-MONOMER; -. DR Proteomes; UP000000807; 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; IPR030940; MG279/MG280. DR TIGRFAMs; TIGR04527; mycoplas_twoTM; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 218 Uncharacterized protein MG279. FT /FTId=PRO_0000210504. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 158 178 Helical. {ECO:0000255}. SQ SEQUENCE 218 AA; 24888 MW; D311BCB120C4C612 CRC64; MIRLLKKLAV FLIILVGILL LGGIATAGYF AFTYREPINN YYKEGYNKIS EYNTEIKKIS QNIFQNNLVK TLSEVEKSLN EGRKLTQNNS FASGLDSSLN ALEGSLKKIN NFDSNAAFTQ IKHTLNNITS FVDQMLEKFP NPNQNDDFKR YLTEVSQILF YTGISIIGAF FVSGFLLILF TKKVYGVRVS RFNPQRLLKK HLVLLLRDEE VYDAVFGN // ID Y281_MYCGE Reviewed; 556 AA. AC P47523; Q49187; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 76. DE RecName: Full=Uncharacterized protein MG281; GN OrderedLocusNames=MG281; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-350. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC 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; L43967; AAC71503.1; -; Genomic_DNA. DR EMBL; U01706; AAB01018.1; -; Genomic_DNA. DR PIR; A64231; A64231. DR RefSeq; WP_010869405.1; NC_000908.2. DR PDB; 4NZR; X-ray; 1.65 A; M=74-468. DR PDB; 4NZT; X-ray; 2.50 A; M=74-468. DR PDBsum; 4NZR; -. DR PDBsum; 4NZT; -. DR STRING; 243273.MgenG_010200002699; -. DR EnsemblBacteria; AAC71503; AAC71503; MG_281. DR KEGG; mge:MG_281; -. DR PATRIC; 20010062; VBIMycGen98045_0323. DR OMA; QSTEYFN; -. DR OrthoDB; EOG6H7FDC; -. DR BioCyc; MGEN243273:GH2R-310-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR030943; M_MG281. DR InterPro; IPR030942; Mycoplas_M_dom. DR TIGRFAMs; TIGR04524; mycoplas_M_dom; 1. DR TIGRFAMs; TIGR04525; prot_M_MG281; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 556 Uncharacterized protein MG281. FT /FTId=PRO_0000210508. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT CONFLICT 348 350 HID -> TLI (in Ref. 2; AAB01018). FT {ECO:0000305}. FT STRAND 82 87 {ECO:0000244|PDB:4NZR}. FT HELIX 95 111 {ECO:0000244|PDB:4NZR}. FT STRAND 116 118 {ECO:0000244|PDB:4NZR}. FT STRAND 120 123 {ECO:0000244|PDB:4NZR}. FT STRAND 125 130 {ECO:0000244|PDB:4NZR}. FT STRAND 135 137 {ECO:0000244|PDB:4NZR}. FT STRAND 140 149 {ECO:0000244|PDB:4NZR}. FT STRAND 154 159 {ECO:0000244|PDB:4NZR}. FT STRAND 176 178 {ECO:0000244|PDB:4NZT}. FT STRAND 181 183 {ECO:0000244|PDB:4NZR}. FT HELIX 187 190 {ECO:0000244|PDB:4NZR}. FT STRAND 191 194 {ECO:0000244|PDB:4NZR}. FT STRAND 206 210 {ECO:0000244|PDB:4NZR}. FT TURN 211 213 {ECO:0000244|PDB:4NZR}. FT STRAND 214 222 {ECO:0000244|PDB:4NZR}. FT HELIX 229 232 {ECO:0000244|PDB:4NZR}. FT STRAND 241 247 {ECO:0000244|PDB:4NZR}. FT HELIX 248 250 {ECO:0000244|PDB:4NZR}. FT TURN 251 254 {ECO:0000244|PDB:4NZR}. FT HELIX 255 261 {ECO:0000244|PDB:4NZR}. FT STRAND 264 273 {ECO:0000244|PDB:4NZR}. FT HELIX 276 280 {ECO:0000244|PDB:4NZR}. FT STRAND 289 299 {ECO:0000244|PDB:4NZR}. FT STRAND 310 316 {ECO:0000244|PDB:4NZR}. FT HELIX 327 329 {ECO:0000244|PDB:4NZR}. FT TURN 340 342 {ECO:0000244|PDB:4NZR}. FT STRAND 348 350 {ECO:0000244|PDB:4NZR}. FT STRAND 361 364 {ECO:0000244|PDB:4NZR}. FT HELIX 366 377 {ECO:0000244|PDB:4NZR}. FT TURN 378 382 {ECO:0000244|PDB:4NZR}. FT HELIX 384 386 {ECO:0000244|PDB:4NZR}. FT STRAND 397 401 {ECO:0000244|PDB:4NZR}. FT STRAND 404 406 {ECO:0000244|PDB:4NZR}. FT HELIX 407 419 {ECO:0000244|PDB:4NZR}. FT TURN 420 422 {ECO:0000244|PDB:4NZR}. FT STRAND 424 431 {ECO:0000244|PDB:4NZR}. FT STRAND 434 442 {ECO:0000244|PDB:4NZR}. FT TURN 445 447 {ECO:0000244|PDB:4NZT}. FT HELIX 449 457 {ECO:0000244|PDB:4NZR}. FT HELIX 459 467 {ECO:0000244|PDB:4NZR}. SQ SEQUENCE 556 AA; 62164 MW; 61DEEB91A8CD0725 CRC64; MQFKKHKNSV KFKRKLFWTI GVLGAGALTT FSAVMITNLV NQSGYALVAS GRSGNLGFKL FSTQSPSAEV KLKSLSLNDG SYQSEIDLSG GANFREKFRN FANELSEAIT NSPKGLDRPV PKTEISGLIK TGDNFITPSF KAGYYDHVAS DGSLLSYYQS TEYFNNRVLM PILQTTNGTL MANNRGYDDV FRQVPSFSGW SNTKATTVST SNNLTYDKWT YFAAKGSPLY DSYPNHFFED VKTLAIDAKD ISALKTTIDS EKPTYLIIRG LSGNGSQLNE LQLPESVKKV SLYGDYTGVN VAKQIFANVV ELEFYSTSKA NSFGFNPLVL GSKTNVIYDL FASKPFTHID LTQVTLQNSD NSAIDANKLK QAVGDIYNYR RFERQFQGYF AGGYIDKYLV KNVNTNKDSD DDLVYRSLKE LNLHLEEAYR EGDNTYYRVN ENYYPGASIY ENERASRDSE FQNEILKRAE QNGVTFDENI KRITASGKYS VQFQKLENDT DSSLERMTKA VEGLVTVIGE EKFETVDITG VSSDTNEVKS LAKELKTNAL GVKLKL // ID Y293_MYCGE Reviewed; 244 AA. AC P47535; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized protein MG293; GN OrderedLocusNames=MG293; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-119. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: Contains 1 GP-PDE domain. {ECO:0000305}. CC -!- SIMILARITY: To glycerophosphoryl diester phosphodiesterases CC (EC 3.1.4.46). {ECO:0000305}. CC -!- SIMILARITY: To M.genitalium MG385. {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; L43967; AAC71514.1; -; Genomic_DNA. DR EMBL; U02118; AAD12392.1; -; Genomic_DNA. DR PIR; D64232; D64232. DR RefSeq; WP_010869413.1; NC_000908.2. DR ProteinModelPortal; P47535; -. DR EnsemblBacteria; AAC71514; AAC71514; MG_293. DR KEGG; mge:MG_293; -. DR PATRIC; 20010116; VBIMycGen98045_0344. DR KO; K01126; -. DR OMA; KPDHYTE; -. DR OrthoDB; EOG6MD930; -. DR BioCyc; MGEN243273:GH2R-329-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:InterPro. 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 PANTHER; PTHR23344; PTHR23344; 1. DR Pfam; PF03009; GDPD; 1. DR SUPFAM; SSF51695; SSF51695; 1. DR PROSITE; PS51704; GP_PDE; 1. PE 4: Predicted; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 244 Uncharacterized protein MG293. FT /FTId=PRO_0000210516. FT DOMAIN 5 244 GP-PDE. SQ SEQUENCE 244 AA; 28913 MW; C501485F56BE47B2 CRC64; MHNKQLLLAH RGYSFIAPEN TKLAFDLAFE YCFDGIELDV HLTKDEQLVI IHDETTLRTA LVNKEVEFES LVSLKRDDHS AFFHLKIQFQ SILTLKEFLD LYLDKFKLIN IEIKTDQKPY LGIEKKLVDL VKGYGKKAID KILFSSFNFE SLQKVYDLDN SYKKGFLFWT KKQFETISTA RIQKICQFLH PWTKIYEKYP QMIKKLNLPL NLWTVNSQNK FQQFLADNHV YAQIANKKFE IKIN // ID Y294_MYCGE Reviewed; 474 AA. AC Q49411; Q49351; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized protein MG294; GN OrderedLocusNames=MG294; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 86-197. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SIMILARITY: To E.coli YihN. {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; L43967; AAC71515.1; -; Genomic_DNA. DR EMBL; U02243; AAA03399.1; -; Genomic_DNA. DR PIR; E64232; E64232. DR ProteinModelPortal; Q49411; -. DR EnsemblBacteria; AAC71515; AAC71515; MG_294. DR KEGG; mge:MG_294; -. DR PATRIC; 20010118; VBIMycGen98045_0345. DR OMA; VNEIRIP; -. DR OrthoDB; EOG6G7R0F; -. DR BioCyc; MGEN243273:GH2R-330-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. 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; Reference proteome. FT CHAIN 1 474 Uncharacterized protein MG294. FT /FTId=PRO_0000210518. FT CONFLICT 191 191 S -> C (in Ref. 2; AAA03399). FT {ECO:0000305}. FT CONFLICT 197 197 K -> N (in Ref. 2; AAA03399). FT {ECO:0000305}. SQ SEQUENCE 474 AA; 52649 MW; 665273D90312D551 CRC64; MIVTTKKGFK KRLKDFSKQQ ILALIILGAI DVFVIAAPYY VKNVVPNLHL YLGITEDEVA TVTSIIGYVT LATQLPGGFL TNRFSSRKLL FLSAITTGAI TFWLAANILT KNQQSHDALF IQYCVIWGLW GITSTLIFWT PLWKLASQQA TKENQALGFG IQGAANGIWG LIFIFLIALI ITSIFYPSGG SENADSKPFA AYAFIIAIML VITGFTVLFF VKEKPIEKQS QTTLVSFKRN LNQILVTLKN WKLWLLSFFL MGMYVFQSTF AYYLLQMLQN AFLAPVVLVT VIGGIRTYAL RSAVSVYLCR LADKCKSYIL FLMICTVLGI VFVLAFILLG FVQTNSANIT LITFSSILYI FTGILSWGMV TVRYNQIGEI DIGKNNYASS VGLLSFIGFS TDGWLYTVTA EVGKKYTVAG QSNTSNTGYQ IIAAICLSIA LFGLICGSIV FISNSMEIKR LNKASYRWRD LDNA // ID Y314_MYCGE Reviewed; 443 AA. AC Q49415; Q49279; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 64. DE RecName: Full=Uncharacterized protein MG314; GN OrderedLocusNames=MG314; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-171. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71536.1; -; Genomic_DNA. DR EMBL; U02151; AAD12432.1; -; Genomic_DNA. DR PIR; G64234; G64234. DR RefSeq; WP_009885988.1; NZ_AAGX01000017.1. DR STRING; 243273.MgenG_010200003240; -. DR EnsemblBacteria; AAC71536; AAC71536; MG_314. DR KEGG; mge:MG_314; -. DR PATRIC; 20010158; VBIMycGen98045_0365. DR OrthoDB; EOG6S52MH; -. DR BioCyc; MGEN243273:GH2R-350-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 443 Uncharacterized protein MG314. FT /FTId=PRO_0000210528. SQ SEQUENCE 443 AA; 51132 MW; 3EFB03F9168015D7 CRC64; MTFSEILTKV QNNLDIVFNN ETLRTRIKTD SDFAKTILAQ LKLLYFLEEK QKRVKTKKPD HFLFGSFHDK FIQLGQNQLS EKELKAAKFD LTDALDLANY LNVAVKNLFN KELNSFTKLA ETQVKPVSEL QENNKTVKDN PSFQTINNSQ QLNSGLENNI LQQTLQVRAR DRAFGRFTSE KLVGKIFEFQ FKSQWIKWAQ LAIFISMIAI FFISIAYVVM VNVFFTHFVD KNSPLFNVNN DQNTVQQSNA DTTNLNRFFA LSSSNLITMI FLAFGGASFF FAFQGKPYSF ATRGQTNRAM RYLRSEFGVK EFPKINDNYR YKVRIKWIFW TIFIFVFLNC IPGNIVRSGF WNAALIIRLF SENQLISVSP LFASYLIGIA WLFVFSIVPF SIISVIAFSL SPKLNLEQTN EIFNKYFQEE LAKPITSDES KTTLDIPPPT IFG // ID Y315_MYCGE Reviewed; 297 AA. AC Q49416; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 73. DE RecName: Full=Uncharacterized protein MG315; GN OrderedLocusNames=MG315; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71537.1; -; Genomic_DNA. DR PIR; H64234; H64234. DR RefSeq; WP_009885989.1; NZ_AAGX01000017.1. DR ProteinModelPortal; Q49416; -. DR STRING; 243273.MgenG_010200003245; -. DR EnsemblBacteria; AAC71537; AAC71537; MG_315. DR KEGG; mge:MG_315; -. DR PATRIC; 20010160; VBIMycGen98045_0366. DR eggNOG; COG1466; LUCA. DR KO; K02340; -. DR OMA; TIHQVIS; -. DR OrthoDB; EOG6CS03S; -. DR BioCyc; MGEN243273:GH2R-351-MONOMER; -. DR Proteomes; UP000000807; 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:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR010372; DNA_pol3_delta_N. DR Pfam; PF06144; DNA_pol3_delta; 1. DR SUPFAM; SSF48019; SSF48019; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 297 Uncharacterized protein MG315. FT /FTId=PRO_0000210530. SQ SEQUENCE 297 AA; 34062 MW; 82BCE69827881C74 CRC64; MTIIYGQDIG LIHQKLSQIK SNSPYKTIWF KDLKQLYDLF SQPLFGSNNE KFIVNNCSFL EKTSLTRQEN LCLEKLKTTD VVLTVYTDNP FSGIKTIKSI TTVFCDKLDW KSMHKAIGEV CRELNLKLDL EIIDWLANAL PLNMGVIYQE INKLSLLGKN EIKDNKLVET VICDYQPVQI YKLTKALTNS QIVKAFKYID ELASTKPNFA TQFLEFFSGE LLLALMVKSC NPKQLTNINL NVNQFRLIAI QSQYHNFTSK VLVNIINAIQ KLDIKLKHND GFAIPLLKNF ALSFFTN // ID Y316_MYCGE Reviewed; 369 AA. AC P47558; Q49466; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 84. DE RecName: Full=Uncharacterized protein MG316; GN OrderedLocusNames=MG316; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7592348; RA Reddy S.P., Rasmussen W.G., Baseman J.B.; RT "Molecular cloning and characterization of an adherence-related operon RT of Mycoplasma genitalium."; RL J. Bacteriol. 177:5943-5951(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To B.subtilis ComEC. {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; L43967; AAC71538.1; -; Genomic_DNA. DR EMBL; L43097; AAA99947.1; -; Genomic_DNA. DR PIR; I64234; I64234. DR RefSeq; WP_009885990.1; NZ_AAGX01000017.1. DR STRING; 243273.MgenG_010200003250; -. DR EnsemblBacteria; AAC71538; AAC71538; MG_316. DR KEGG; mge:MG_316; -. DR PATRIC; 20010162; VBIMycGen98045_0367. DR eggNOG; ENOG4107I0B; Bacteria. DR eggNOG; COG0658; LUCA. DR OMA; LATWIPY; -. DR OrthoDB; EOG647TWC; -. DR BioCyc; MGEN243273:GH2R-352-MONOMER; -. DR Proteomes; UP000000807; 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; IPR004477; ComEC_N. DR Pfam; PF03772; Competence; 1. DR TIGRFAMs; TIGR00360; ComEC_N-term; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 369 Uncharacterized protein MG316. FT /FTId=PRO_0000210532. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 47 67 Helical. {ECO:0000255}. FT TRANSMEM 119 139 Helical. {ECO:0000255}. FT TRANSMEM 152 172 Helical. {ECO:0000255}. FT TRANSMEM 206 226 Helical. {ECO:0000255}. FT TRANSMEM 235 255 Helical. {ECO:0000255}. FT TRANSMEM 272 292 Helical. {ECO:0000255}. FT TRANSMEM 296 316 Helical. {ECO:0000255}. FT TRANSMEM 323 343 Helical. {ECO:0000255}. FT CONFLICT 120 129 NIVHLFVISG -> KHCPFVCYQW (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 369 AA; 43195 MW; 96D9BF1F90F6FFF0 CRC64; MQTKLFYFFV LLSFIPGFFL VQQEQFVALS IWIILITLFS LWYDWKFCLL NLTIVGFFIA FCYFVPAVKI NQIVKNNFIR TPFINWIDQT TKGELNQYLK LFLINETTKN NLYQNALKLN IVHLFVISGF HLSFLFNLME RFLWKRWYLN KLSGFAVLLI YLFLVGFAFS ALRVFISTLL KQVFKKQLPE DNLSLTALLI ILISNHALNN FGFNFSFLAC FVLLFVNKLK LLKALKPLVS SSLILIVISP LSLYLNSRLN AFSVLFNLLF SPIALFYFCV SWIILPFIGV FGQASFGIYL PLKMLSEWSL KVTVFLQIPK PNLIFFFVYY GLLGLLYTIF TVAYYDNNLW SRYWANSPKI KSNQKQFSI // ID Y319_MYCGE Reviewed; 178 AA. AC P47561; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 76. DE RecName: Full=Uncharacterized protein MG319; GN OrderedLocusNames=MG319; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7592348; RA Reddy S.P., Rasmussen W.G., Baseman J.B.; RT "Molecular cloning and characterization of an adherence-related operon RT of Mycoplasma genitalium."; RL J. Bacteriol. 177:5943-5951(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-141. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43097; AAA99944.1; -; Genomic_DNA. DR EMBL; L43967; AAC71541.1; -; Genomic_DNA. DR EMBL; U01769; AAD10587.1; -; Genomic_DNA. DR PIR; C64235; C64235. DR RefSeq; WP_010869428.1; NZ_AAGX01000013.1. DR STRING; 243273.MgenG_010200003018; -. DR EnsemblBacteria; AAC71541; AAC71541; MG_319. DR KEGG; mge:MG_319; -. DR PATRIC; 20010168; VBIMycGen98045_0370. DR OMA; DVFNRFF; -. DR OrthoDB; EOG6S7Z3T; -. DR BioCyc; MGEN243273:GH2R-355-MONOMER; -. DR Proteomes; UP000000807; 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 1 178 Uncharacterized protein MG319. FT /FTId=PRO_0000210534. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. SQ SEQUENCE 178 AA; 20556 MW; 1BCC5FDA9DA4AE14 CRC64; MRLFRFLFKL CFLLLVLVGF AYLFLAIFYF GSLNPFELAQ PMDVFNRFFS KEALDNISSN NGATATAQTS SLLQLLEGSS NGLDNRFPTE KSAFYAIPGY VDFLKNAKLP GFVEQFTPYL TKYVIPLGMA FVSGLIGTLI VNFFLNKITR SIKRRKRNMK KQEQEEYYDD SRSRRKRN // ID Y323_MYCGE Reviewed; 227 AA. AC P47565; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 85. DE RecName: Full=Uncharacterized protein MG323; GN OrderedLocusNames=MG323; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Contains 1 RCK C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00544}. CC -!- SIMILARITY: Contains 1 RCK N-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00543}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71545.1; -; Genomic_DNA. DR PIR; G64235; G64235. DR RefSeq; WP_010869432.1; NC_000908.2. DR ProteinModelPortal; P47565; -. DR STRING; 243273.MgenG_010200003043; -. DR EnsemblBacteria; AAC71545; AAC71545; MG_323. DR KEGG; mge:MG_323; -. DR PATRIC; 20010198; VBIMycGen98045_0376. DR eggNOG; ENOG410865Q; Bacteria. DR eggNOG; COG0569; LUCA. DR KO; K03499; -. DR OMA; QLAKMNC; -. DR OrthoDB; EOG6HQSSJ; -. DR BioCyc; MGEN243273:GH2R-368-MONOMER; -. DR Proteomes; UP000000807; Chromosome. 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; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006037; RCK_C. DR InterPro; IPR003148; RCK_N. 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 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 227 Uncharacterized protein MG323. FT /FTId=PRO_0000210539. FT DOMAIN 5 126 RCK N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00543}. FT DOMAIN 134 221 RCK C-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00544}. SQ SEQUENCE 227 AA; 25494 MW; 194FA48B5F0C82AF CRC64; MKRADFCIIG LGRFGMQVAQ SLKENNFNLL LIDLDDKKTD TASQQFDYVI CCDASNLTAL EELQIDEFAG VIVGVTNIEA SIMICANLRE LGQKNIIAKA KNEVHKRVLS TMGIREALIP EKIVGKNLVI RLIHGLENEI INLGNEIIFI RSAVNNKAFF NKRLEEINFR QNTDANIISI MRSNKTVVFP LGPNTEIQPG DIITAVCQQK SLNKYLNYIN PKTKNKN // ID Y384A_MYCGE Reviewed; 149 AA. AC Q9ZB71; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 73. DE RecName: Full=Uncharacterized protein MG384.1; GN OrderedLocusNames=MG384.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. 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; L43967; AAC71616.1; -; Genomic_DNA. DR EnsemblBacteria; AAC71616; AAC71616; MG_524. DR KEGG; mge:MG_524; -. DR PATRIC; 20010354; VBIMycGen98045_0450. DR OMA; FFLIRSK; -. DR OrthoDB; EOG664CF9; -. DR BioCyc; MGEN243273:GH2R-441-MONOMER; -. DR Proteomes; UP000000807; 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; IPR020375; Uncharacterised_MG384.1. DR ProDom; PD077269; Uncharacterised_MG384.1; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 149 Uncharacterized protein MG384.1. FT /FTId=PRO_0000210584. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. SQ SEQUENCE 149 AA; 17731 MW; F0A7A8DDD2562384 CRC64; MGKEIEPIFD LVLLWFLFVP LLIYLFLAFF LFAFTKYIIW ELIPFCYSTA FTLIVLFLSG IIPMAWNSWI ILLRFFLVLI TLMLSFFLLN KMTNFFLIRS KYAIIIAENL LKTGKSKTKN RQKLQQIQSD LERKKSAEIV FKIKKKKPK // ID Y395_MYCGE Reviewed; 524 AA. AC P47635; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Uncharacterized lipoprotein MG395; DE Flags: Precursor; GN OrderedLocusNames=MG395; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-152. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 255-326. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG067/MG068/MG395 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; L43967; AAC71623.1; -; Genomic_DNA. DR EMBL; U02260; AAD12525.1; -; Genomic_DNA. DR EMBL; X61530; CAA43742.1; -; Genomic_DNA. DR PIR; G64243; G64243. DR RefSeq; WP_010869465.1; NZ_AAGX01000001.1. DR STRING; 243273.MgenG_010200000535; -. DR EnsemblBacteria; AAC71623; AAC71623; MG_395. DR KEGG; mge:MG_395; -. DR PATRIC; 20010376; VBIMycGen98045_0461. DR OMA; TGWLFDW; -. DR OrthoDB; EOG6N9469; -. DR BioCyc; MGEN243273:GH2R-452-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022382; DUF31. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR022381; Uncharacterised_MG067. DR Pfam; PF01732; DUF31; 1. DR PRINTS; PR00840; Y06768FAMILY. DR SUPFAM; SSF50494; SSF50494; 3. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 26 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 27 524 Uncharacterized lipoprotein MG395. FT /FTId=PRO_0000018737. FT LIPID 27 27 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 27 27 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 524 AA; 60932 MW; 0CB9913D7DD717D6 CRC64; MLKIDMWFKL KSLGFSLISL QALLASCSAV SPVPVPIEEK NDSTTDNNAT PFKDEQSDQG TEVNQQPKVE QKVYNRNFKF NTSFIPEESD IYRKGYDLTF TLNFTSFSND SYGTGWLIDW KGDENTTQKQ GSFFAYIATN LHVADGLRNI GDHWPYSKTD DQREFNEYES TVYFSIGKYT NKTDITKLYQ EEKLEQRKVN DSLLSIQTSN IPKTAYTATN FLKGVNSIKP VYADFAVIEL ELNLENLRDW QIFNEFIKPA INTYKSLGDS TNIFETKDLE QHWNHSHYLL GYPVLERGYD QNRLLEQKEE FARTHNFNQK SQLWSKNTYL VSTAKEIPVI TKNARKDGQI GSEIFSKKTQ DSHVDKVIKH EKGIVTFQNF KNFKLKYHDK EYQQYGYGLM LDDTNLPGGS SGSAIFNNNQ KINSIYFGVL EVYKNSKTHK DNIGMSQLLR TSKRESEKNK TRTTNNRDKF QHYDLIFGDS NTKSFYAQFA KKHNTHLYDQ IKSSEKEEFK YVDKNNQKTP FLLR // ID Y412_MYCGE Reviewed; 377 AA. AC P47652; Q49510; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Uncharacterized lipoprotein MG412; DE Flags: Precursor; GN OrderedLocusNames=MG412; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74 AND 189-225. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB01014.1; 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; L43967; AAC71640.1; -; Genomic_DNA. DR EMBL; U01702; AAB01014.1; ALT_INIT; Genomic_DNA. DR EMBL; U02101; AAD12373.1; -; Genomic_DNA. DR PIR; F64245; F64245. DR RefSeq; WP_010869472.1; NC_000908.2. DR ProteinModelPortal; P47652; -. DR EnsemblBacteria; AAC71640; AAC71640; MG_412. DR KEGG; mge:MG_412; -. DR PATRIC; 20010416; VBIMycGen98045_0481. DR KO; K02040; -. DR OMA; CANINLI; -. DR OrthoDB; EOG6HB9P1; -. DR BioCyc; MGEN243273:GH2R-469-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR024370; PBP_domain. DR Pfam; PF12849; PBP_like_2; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 23 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 24 377 Uncharacterized lipoprotein MG412. FT /FTId=PRO_0000014040. FT LIPID 24 24 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 24 24 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 377 AA; 42470 MW; DD7E9BE19EBA70F2 CRC64; MLKFRNFFKL TLLTLASAFF LSGCANINLI SAVGSSSVQP LLNKLSSYYV LNENNDNDKL VEISVQAGGS NAGIRAIING FADIGNVSKN PKEYAKENEK KWRDKKLKTL TIGKDAIAVI YKAPQELKGK LLLTKDNIND LYDLFAGVKT INIDKFVKKD TKNMSNEKDY PLTSFPRTGG SFASGTAEAF LNFSALKSDK TLDSQTRDIL KGIINYGPLA KPTSETNIEA FNTFVTNLQD PNLFGMIYLS LGFIQNNLQA IKNNGFEILP IKYENKEVLP SNQTVSQNEY KWVRPLNSIV SLSEENKNID EIKTFFNWLF FNGKKDVIKN IYDEFGILQL TEDEKKKMFK TNDSSPMNLE NFWVDDFAFS NPIFGAF // ID Y423_MYCGE Reviewed; 561 AA. AC P47662; Q49470; Q49480; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Uncharacterized protein MG423; GN OrderedLocusNames=MG423; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 55-138 AND 400-478. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 486-561. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71647.1; -; Genomic_DNA. DR EMBL; X61510; CAB97509.1; -; Genomic_DNA. DR EMBL; X61524; CAB98129.1; -; Genomic_DNA. DR EMBL; U02228; AAA03380.1; -; Genomic_DNA. DR PIR; G64246; G64246. DR RefSeq; WP_010869479.1; NC_000908.2. DR ProteinModelPortal; P47662; -. DR EnsemblBacteria; AAC71647; AAC71647; MG_423. DR KEGG; mge:MG_423; -. DR PATRIC; 20010432; VBIMycGen98045_0489. DR KO; K12574; -. DR OMA; PWLLMKI; -. DR OrthoDB; EOG6PCPSF; -. DR BioCyc; MGEN243273:GH2R-477-MONOMER; -. DR Proteomes; UP000000807; 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:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR004613; RNase_J. DR PANTHER; PTHR11203:SF22; PTHR11203:SF22; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR00649; MG423; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 561 Uncharacterized protein MG423. FT /FTId=PRO_0000210604. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TRANSMEM 80 100 Helical. {ECO:0000255}. FT CONFLICT 136 138 PFK -> LLR (in Ref. 2). {ECO:0000305}. FT CONFLICT 403 403 A -> R (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 561 AA; 63397 MW; 5FE18E9D7BDC9FEA CRC64; MAKIKFFALG GQDERGKNCY VLEIDNDVFI FNVGSLTPTT AVLGVKKIIP DFSWIQENQA RVKGIFIGNA ITENLGSLEF LFHTVGFFPI YTSSIGASII KSKINENKLN IARDKLEIHE LKPLETIEIS NHSITPFKVS SSLPSSFGFA LNTDNGYIVF IDDFIVLNDK NIAFENQLNQ IIPKLSDNTL LLITGVGLVG RNSGFTTPKH KSLEQLNRII TPAKGRIFVA CYDSNAYSVM TLAQIARMQN RPFIIYSQSF VHLFNTIVRQ KLFNNTHLNT ISIEEINNST NSIVVLTSPP DKLYAKLFKI GMNEDERIRY RKSDTFIFMT PKVAGYEEIE AQILDDIARN EVSYYNLGRE ILSIQASDED MKFLVSSLKP KYIIPTGGLY RDFINFTMVL KQAGAEQNQI LILFNGEVLT IENKKLDSKK NELKLNPKCV DSAGLQEIGA SIMFERDQMS ESGVVIIIIY FDQKKSEFLN EITYSFLGVS LDVPEKDKLK TKMEELIKKQ INDIKDFTTI KKRIGKEISK ELKVSIKRAV MNLFTKMTSK APLILSTIIS I // ID Y439_MYCGE Reviewed; 272 AA. AC P47677; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=Uncharacterized lipoprotein MG439; DE Flags: Precursor; GN OrderedLocusNames=MG439; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 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; L43967; AAC72459.1; -; Genomic_DNA. DR PIR; E64248; E64248. DR RefSeq; WP_009885595.1; NZ_AAGX01000001.1. DR STRING; 243273.MgenG_010200000270; -. DR EnsemblBacteria; AAC72459; AAC72459; MG_439. DR KEGG; mge:MG_439; -. DR PATRIC; 20010462; VBIMycGen98045_0504. DR OMA; LLENPMD; -. DR OrthoDB; EOG69PQBN; -. DR BioCyc; MGEN243273:GH2R-492-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 20 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 21 272 Uncharacterized lipoprotein MG439. FT /FTId=PRO_0000014042. FT LIPID 21 21 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 21 21 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 272 AA; 30496 MW; B69C882528723988 CRC64; MKLRKIFLLP LISLSTLSVA CSSTDPGLEK AQAYFQRNNI ELSKNNAVTF LKKGYSSDKE EVINTVFASW KTTLLDYQLL EKPLDYSRFA KAFGVNKSKE DVTPNISAKG LYFDETYPGI SGQIALVLGV KSQKVVNFQY SWKNNLDFKV QIHLKMTGIV GSDNTSTSLI KSFLASTSGV SESDFTGDKA NFDGDVIFTY TPPTDNRRVS ESTFSSIPAS INFPFDIKID MSTSHEKLNL LLSTNEQVKK IRTRTFKGKS IDLLPFFYYT LL // ID Y468_MYCGE Reviewed; 1783 AA. AC Q49460; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 3. DT 13-APR-2016, entry version 87. DE RecName: Full=Uncharacterized ABC transporter permease MG468; GN OrderedLocusNames=MG468; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 879-985. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC-4 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; L43967; AAC72488.1; -; Genomic_DNA. DR EMBL; U01808; AAD12339.1; -; Genomic_DNA. DR RefSeq; WP_009885565.1; NZ_AAGX01000001.1. DR STRING; 243273.MgenG_010200000075; -. DR EnsemblBacteria; AAC72488; AAC72488; MG_468. DR KEGG; mge:MG_468; -. DR PATRIC; 20010530; VBIMycGen98045_0538. DR eggNOG; ENOG4105NZ9; Bacteria. DR eggNOG; ENOG4111U52; LUCA. DR KO; K02004; -. DR OMA; YPKLANI; -. DR OrthoDB; EOG69GZN1; -. DR BioCyc; MGEN243273:GH2R-521-MONOMER; -. DR Proteomes; UP000000807; 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 InterPro; IPR003838; ABC_permease_dom. DR Pfam; PF02687; FtsX; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 1783 Uncharacterized ABC transporter permease FT MG468. FT /FTId=PRO_0000210631. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT TRANSMEM 917 937 Helical. {ECO:0000255}. FT TRANSMEM 967 987 Helical. {ECO:0000255}. FT TRANSMEM 1010 1030 Helical. {ECO:0000255}. FT TRANSMEM 1084 1104 Helical. {ECO:0000255}. FT TRANSMEM 1660 1680 Helical. {ECO:0000255}. FT TRANSMEM 1709 1729 Helical. {ECO:0000255}. FT TRANSMEM 1730 1750 Helical. {ECO:0000255}. FT TRANSMEM 1752 1772 Helical. {ECO:0000255}. SQ SEQUENCE 1783 AA; 200168 MW; 87BD575AEC2E374B CRC64; MFSFFKQIFK SLKKFFFLLF GIIFVLFSII FLETSIVQLS NNLVSTYTTL VSKTNSSDIV APAILKEANP VYIASLTNDS GYFSKIKIDD KKINYLFPYQ ENDFGSDSGQ SNGSGDNQNK TIPRKGDVNE KDKLFLARKR GILKAYGEAN IAEKRIYKGL AVSFNNTDSF NGSDISDSIT NRHIISDPQN LIYDASGNLL GYFADGLIKE TISLRAGIAR FPGDKGKSTG TQVKITQKQQ TNNDPQKDST VNSLYKTNNK DKVWFKSDET KADNTDISAN YLFTGGNEAA NWFPNLYANI PIDLEIDPGS QFWKDVNPFK EIVEEFQTQK ESKDNQSFTL TFNLDISKLN KLDNEQLKWL ETNAKTIANN SSFGDWDLEN KLKQLKKFEL KINKDWLKKK VESEKDTILN SLPGFSDSDK DTIFKTQNGM MVRNNNLSFQ PSSNNLQLVQ NQNSQASNGI ADPNFSNVQT AYNKIHQSNN TPEKTLDAVY AAVLDQWRSI FQEDLVKKTV DLLEKYRDHF LKATAFNNID YSKQNIAIAN NVSSAESASF LVSNKDEQRY NDLSLIDGVD LKSWLFKPEQ NESNPLDTIY GGQDANNGFL QKIDYEFKPS TSSGGMTASL KNTQALSPKS TKFPIYPKLA NIIAQAQLPE ATNIPTTALD ALKQWTNLDA NGFNNLKEED KRKAANNYLA LLSYFTPAFQ DPNELIETNR QMLEIPITVK NGVNPLILPT DQQNLVVQTP EAHGAVVSQQ WLFRHNKEIL PQEGEYAWKT ALQTPNNFPN WLNDLPDRYK FSINGLTFAI LGIGESVETG YPVLSLQSPL PNTQDEALIF VNDQAYRSIL FAVPAANQEN YYAFKSTDLK QHTDQDPVQF IANRLEGYLD VPRSDLAFNV KDISKFNYLT TARNYFPDLV QSYLAIVSTV IAIFLIILAL YLIILLIKSF IKKNQTEFSI IRAGGFSTTK FIVGMSVFAG IVAIVSSFLG VLFAFLLEGQ VKGIINRYWF IALPENSFNW LSFFGSFFIT FFVFEFISWI AFKQLFSKPV NVLIDQGNET KFSVLLHLLK HKSHTMSPLT KFRVSLIVSR FSRLFTYVGL SSVALLLIGI AGTIPQKFSA AQTSTSLNRN FNYKLNLQTP TEQSGWYAIQ PYSHFGVTDN NNGIKTLYNE SVQANSQNEH PYKPSNLKLK NRQDQPIKAA DGTELELGNL LLPSYGGAQQ LNTDENFFRH ASLSKWIIDF PIRVGGSNIN PWEIVEKSIP KQITQLLSAS SDQFLISVLT DDFFNNLNAN GFLIRNPRTN QIQLDASRVL TTIDVFNPGG VKFNDSFLSF MLKVYGDFEL AKQDSKLNFG IVPVDPAIEE TYTYVEGPFG FQEDNLDENS PYTLTGINPE SSFVNLIDGS GNSLRNLISS DQEMNVIVNA GFQYANNINI GDYVYIKPKN TATRYSEKFL KAPLNNSTVA FKVVGVSTDA FGQELYINQH IANNLLKLSG NQGRGIIRDV IKKTNGQSQS SDEYEIDYVK PNGYVPFNGV FSKELKPSLL NKALVLNSII GVWGNFTDFG NNFQNLVRNK LDKVITSILP TDPEIINKLA QEKQIINTTS MNYESLRKEL VNKYKTEWNS VNLLSQNASS IFGNNIIAPV LNIDAAGTSA QIIRNNAEVL FNTVNQVDAF LLGTIIPFIF ITCVVLGISM LEEMKRIFIS LKAIGYRDVQ NLISLLTFFI PAFVLALLIS IGVLAGVLIG IQAVVFNVAQ VFLTNVFEFL PYMVGIVLFG VTIFVIGSYF WIKLRSAELK EGF // ID Y284_MYCGE Reviewed; 132 AA. AC P47526; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 56. DE RecName: Full=Uncharacterized protein MG284; GN OrderedLocusNames=MG284; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71506.1; -; Genomic_DNA. DR PIR; D64231; D64231. DR RefSeq; WP_010869406.1; NC_000908.2. DR STRING; 243273.MgenG_010200003290; -. DR EnsemblBacteria; AAC71506; AAC71506; MG_284. DR KEGG; mge:MG_284; -. DR PATRIC; 20010080; VBIMycGen98045_0327. DR OMA; WNENDIN; -. DR OrthoDB; EOG6XHC67; -. DR BioCyc; MGEN243273:GH2R-318-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 132 Uncharacterized protein MG284. FT /FTId=PRO_0000210510. SQ SEQUENCE 132 AA; 15392 MW; E70000287B2C5F62 CRC64; MTFTNKEKNC KQSKSLAALM TKFKRSQLIL KHQANNIALE LWNENDINLS KQLIELIEDT FSMLKKETVD FIYDIYIYGK KPCDIGYSNS TYYKKLNKAA NSFFDHFVWD SSILDKRIIT NGSNSQRTTN SK // ID Y309_MYCGE Reviewed; 1225 AA. AC P47551; Q49317; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized lipoprotein MG309; DE Flags: Precursor; GN OrderedLocusNames=MG309; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1138-1224. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; L43967; AAC71531.1; -; Genomic_DNA. DR EMBL; U02200; AAD12488.1; -; Genomic_DNA. DR PIR; B64234; B64234. DR STRING; 243273.MgenG_010200002534; -. DR EnsemblBacteria; AAC71531; AAC71531; MG_309. DR KEGG; mge:MG_309; -. DR PATRIC; 20010148; VBIMycGen98045_0360. DR OrthoDB; EOG6TXQRZ; -. DR BioCyc; MGEN243273:GH2R-345-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022186; DUF3713. DR Pfam; PF12506; DUF3713; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 27 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 28 1225 Uncharacterized lipoprotein MG309. FT /FTId=PRO_0000014032. FT LIPID 28 28 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 28 28 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CONFLICT 1185 1185 L -> V (in Ref. 2; AAD12488). FT {ECO:0000305}. SQ SEQUENCE 1225 AA; 138376 MW; C3E4BF5B4319B6E8 CRC64; MKRFLHRVKW PLLLSSIAVS LGIVAVACAQ PNSRTIENLF RPSSAFTDKN DGSINATLYK ALENREGLTQ YLTMRLAPVL RNFYEENVDD DIKRNLRTFN TDTDNSFVNQ EQNLRNQYRG DYLVRLQTDI LDNTGGNQAN WKLRDVNNKI VDDFINKLFT KNFVEYVDKS VGVLSTPLKG LIENQSNWNN IKIQAKFVDK NKRLRINNDA VYAAIQDKLL DQFVTNENPN LVSRVVFTNE TPNDGFDNYF NPDLIKSPTP SYQFQVFNKY NQQDNSIKGA NGFHILASNL QSYVNTNNKT IDIPNKFSSD SGGKLLLKAS DMFDTFDPSF SAAFIQGYLA LQKKSKGAEQ TEYTKLEKDK SIIENFFVEN NSAKAAMKSA SSSSQTTTVH KTDLAKIFKE NETTKSTDVF KGEYQKKFSN ATSTSNSDSS NNSAIVDLKE LKKDNNSQPD LILARGKDGI HLMGVDGGGY YLSESGRDVN KQKQFLLFRA LQTKYGLIDT NTTYDFKLFD EVKKHFDKNR VLFLFNALFK LVDSKESNFL SFPQFKKFSD SIITVKNELK DLVESQYQQI VFNEVATAEN KVALKLAERN QPFIDNERNK QIWMNGLAAV LPYEQDSKTG HYNELGIYYK DIIDKVSSNT SNSNSNSNSS SSDPFSKKII DKLKENKKKV EAAVKKHVDE LKVSVIPSPQ YSQIILVDTK LSSDPRNTSL ALNLALNAVL SSDELQNTIR RDYFVNDDQF KQAIDLDKLT FKNWNSLNNE NWNIFKYTYL FDLFQKQANP SIFGNGVNES STDNKPKING VLDSLYNSLN LEERLDSNDL INYYSYLYTV QWLLKDNLKN LKQDLQAKLS RTTNSFLVWS LASDKDRNNT ASQAMSVSSS KSVLVKMANN VASQTNQDFT KQEQQNPNYV FGSSAYNWTN NKTPTVNSAA NDISSLYYTK NNGSSSTSLT LMQKSAQQTN NQQRRFGFHG IVTNTSSNNL PDAVRNRLFT SFVSQSEKSS SNGGQAQLQS TQSSGSNETI YKGALFSFGS LTKLIETIDN IPTQAEFDAL YNHLTSNLNI NVTGVDRSKS LQEQKTNLKN FANSNFNNTQ TVQLKQAQSK TNNSNFNDVF SRFEGYIGTN KTSNYSSYNF LQDNQIYHAV YAKQINLEDV SMLGSDSLNS TDSNNSKRLD LSLEEFLSTV ALEALNPNNQ TQAINALIAN AKNGLVRVGD NRLFSAISSQ WVRKF // ID Y323A_MYCGE Reviewed; 269 AA. AC Q9ZB74; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 72. DE RecName: Full=Uncharacterized protein MG323.1; GN OrderedLocusNames=MG323.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. 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; L43967; AAC71548.1; -; Genomic_DNA. DR STRING; 243273.MgenG_010200003053; -. DR EnsemblBacteria; AAC71548; AAC71548; MG_515. DR KEGG; mge:MG_515; -. DR PATRIC; 20010202; VBIMycGen98045_0378. DR OMA; YLFYSRF; -. DR OrthoDB; EOG6JDWF7; -. DR BioCyc; MGEN243273:GH2R-371-MONOMER; -. DR Proteomes; UP000000807; 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 1 269 Uncharacterized protein MG323.1. FT /FTId=PRO_0000210541. FT TRANSMEM 64 84 Helical. {ECO:0000255}. FT TRANSMEM 125 145 Helical. {ECO:0000255}. FT TRANSMEM 169 189 Helical. {ECO:0000255}. FT TRANSMEM 230 250 Helical. {ECO:0000255}. SQ SEQUENCE 269 AA; 31589 MW; AAEEC20C3CB1A22F CRC64; MLKKKNQFDY LNLSHVLSKK KNSGGGWINK ISDKLSEINV AEYQVVSKHS NYLFYSRFGL LDTFVYFLFF LCFFLNNVLF LAGVFHTKQF TFNEVNGFNQ FYLFWTVEKP TDIIQASITY QISQYGIANL VFGLISLALL VFLSFRWTVS LFFKSQTTKW ERIGYTTGFF ISIVVYLLWI LLMVLFLVLL DQQFFERDTQ KIQSATRFSL FFNVENNNGV YLSKLNSFGV FATAWAISLV FYSFFFIAIF AFNYNKTKLK QLFKKSKAK // ID Y328_MYCGE Reviewed; 756 AA. AC Q49419; Q49308; Q49320; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 69. DE RecName: Full=Uncharacterized protein MG328; GN OrderedLocusNames=MG328; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-113 AND 155-272. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71552.1; -; Genomic_DNA. DR EMBL; U02203; AAD12492.1; -; Genomic_DNA. DR EMBL; U02188; AAD12472.1; -; Genomic_DNA. DR PIR; C64236; C64236. DR RefSeq; WP_010869434.1; NC_000908.2. DR ProteinModelPortal; Q49419; -. DR STRING; 243273.MgenG_010200003190; -. DR PRIDE; Q49419; -. DR EnsemblBacteria; AAC71552; AAC71552; MG_328. DR KEGG; mge:MG_328; -. DR PATRIC; 20010212; VBIMycGen98045_0383. DR eggNOG; ENOG410XP6Z; LUCA. DR OMA; KTHECAS; -. DR OrthoDB; EOG6N3CNZ; -. DR BioCyc; MGEN243273:GH2R-376-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 756 Uncharacterized protein MG328. FT /FTId=PRO_0000210543. FT CONFLICT 52 52 T -> R (in Ref. 2; AAD12472). FT {ECO:0000305}. FT CONFLICT 65 65 S -> W (in Ref. 2; AAD12472). FT {ECO:0000305}. SQ SEQUENCE 756 AA; 88407 MW; 1D3AD4EF0AB5C068 CRC64; MAVDKELEIS DFDNELDEKT LLKELVQRTN NILFSPSKIT AIPFERNLLE KTFFGTVDEA EKEKSIVSFF NWMIDLKVLD KKWDKNVLNH YANQLKTREE EQQTVDQTMA FQEVDDQSVL TKEIKTGFQE LKPSVITAED DKDEIKPEAT KQVSFEELFN QPSEEINETK KPEVQIFSTD KVKEPEQFDD FYSIENLTKA INPVHKTIQY DQNDDQPFVV KRILKEQHPT KKVDELDDYN NKELLLENAD LKKQIDDLKE NNNDQIFDLE QEIDDLKRRL SEEKSKHLHT KKLQDDLLQE NRDLYEQLQN KPVAINPLSD EVNEELENLK QEKALLSDQL DALKNKSSNV QQQLALLPVL NNQINELQNQ LLTAREANQR LDLVEQENDF LKNELKKLHD NTSNDENEKY DDLLNQYELL FDENETKFDK LQVKQQALNL DYQKTISALK HENDVLLDEI EWTRSKDNDF NNTKNSFEEQ KKALDEKLNG LTIQNQQLQD KIAELEEWNE EKSNLNTNQL VNLQQQLKDS QNLFNVAQDK LATLEEVNLA LNEKINDLED ELSGSENSNN LLAKLQADHE ILQESYGKLK TDFEKLKKNK LNDANEQYQD LLSAFEETNS ELEKAKQSLS ASDSENNQLK QQINSLENAK KELQFTPVTS DEHLDELETL KIEKEQLFLE NQALQNQLQY FNDISANQTE EIKEASDEDK PVEIKKPRIK KRDFVIQNKD DKLAKLSKKE RIQAYAERLA KINANE // ID Y338_MYCGE Reviewed; 1271 AA. AC P47580; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Uncharacterized lipoprotein MG338; DE Flags: Precursor; GN OrderedLocusNames=MG338; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1023-1114. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG307/MG309/MG338 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; L43967; AAC71563.1; -; Genomic_DNA. DR EMBL; U01809; AAD12341.1; -; Genomic_DNA. DR PIR; D64237; D64237. DR STRING; 243273.MgenG_010200003131; -. DR EnsemblBacteria; AAC71563; AAC71563; MG_338. DR KEGG; mge:MG_338; -. DR PATRIC; 20010236; VBIMycGen98045_0395. DR OrthoDB; EOG6TXQRZ; -. DR BioCyc; MGEN243273:GH2R-388-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022186; DUF3713. DR Pfam; PF12506; DUF3713; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 26 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 27 1271 Uncharacterized lipoprotein MG338. FT /FTId=PRO_0000014036. FT LIPID 27 27 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 27 27 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 1271 AA; 142492 MW; FCE6042067310A70 CRC64; MAHRFKRWSL IALAFSGVGA TAIITACSTI NTANLFPTLN RSQKLIGFSD QNIINPDVVL KSALNDGSGV DSILRVSFGS ALQKWYQANA DRNISNRLKI FEENVEDEHD NLIDEKKRAD RVKWPIEVQK EYDQFGGNQE SWKKLKLYDR LITDFQSLIF NNISANVSLV NSSDTSVATT KENIEKTENK LKFINSNLND VNGDFFTNLQ AYLFSQWLIE ENPFLLNQAS FNYQSPIAGL GSIYDENAIG ASNLNLSYNF PAFQDPSESG GQTNSAKLFE EFDKQLQTAN SSGSSQSSAA TNTRNDLLDF ENKYSASKVL ISKNNILSVL KTVNLSAAVI DQYHYLLNNK TELTTTTTTT TTTTGGTSSN LNPLDKFIKS SSATTVMMKS AMTKSQEVTS DNNGFNVKSE FLKINPSLSS SGSDNSSNTQ SFWKQVQALN NSSQTATIFD AVRMESNSSQ AQVVTSNLLV SLSSKTTQKQ QQKPVYVRGD DAIYAFHIDG GNYFLENSSP NKRNFEKQAE VLLMRFLQGQ TNNFSKDNVS FSVDLFGSNS EFRSWANRNT TLKLYTALTT MLENGTSNNN GQKDVCDLAK KLLKNNTNLS ETIKKQQDFN NSLSQIKSSY ESYIKAANKL NNFRTDLANI EKLEQAIVDR ANNYIKLQKE AKESSIGWGQ PLPYKRANDG SYPSLAKFFN NNSDQSSAQT LTLKTTAAAI TSDNEPTREK NNQTLKTLTT EVENKAKELV EKWKATTYSS SQYSEIITLK SSQLNDLDLD LILSLLTDSG IRTGTVANIF KNWYFKNTNS FTNNFDTSNK ELKGEFSDFN DLVKQALYIR SWQNLTSKER FGYYKDLGSV NSTSTMLQMQ NKAAQSHTSS SVNQTLLDLA KKAFEKELED PNQDAEYKYM RFLQALMWLV KNGAQNYKNL LQQAIPIGTR AFVSWTVGYD KNPSATVSQK TKSSTSSANE NPFNRFLQNP NYTQGSEINW FNDKQTPIQP DSLLESENTY RFTDEPFNNS VALSNKSQGS SDKKYFYGFN GLTINSNQSI STASAGLTQQ LFNNYGQLIT ATDKAGALSQ YKDKFTLWSL INKTSSDAEL NAFGELLHRS VNVDTNNLSR FNSRGEPLIS FDNKKKFLLN VVDRLDDLYF HKFEGYVGLS KAANTDGSNT EGYKTVQTVP LTNDSSIQTL SYVIQITNDD VNKISSNWKN NKANSLGLKK EIFMSLLIEQ ALDEGTQELA FLDLIRENQK QHQREHQQIL VGDKRLYDIL GQTLAINAKN F // ID Y389_MYCGE Reviewed; 127 AA. AC P47629; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 67. DE RecName: Full=Uncharacterized protein MG389; GN OrderedLocusNames=MG389; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-106. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC 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; L43967; AAC71617.1; -; Genomic_DNA. DR EMBL; U01813; AAD12349.1; -; Genomic_DNA. DR PIR; A64243; A64243. DR RefSeq; WP_009885633.1; NZ_AAGX01000001.1. DR STRING; 243273.MgenG_010200000570; -. DR EnsemblBacteria; AAC71617; AAC71617; MG_389. DR KEGG; mge:MG_389; -. DR PATRIC; 20010364; VBIMycGen98045_0455. DR OMA; WYNITIM; -. DR OrthoDB; EOG6QP199; -. DR BioCyc; MGEN243273:GH2R-446-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 127 Uncharacterized protein MG389. FT /FTId=PRO_0000210590. FT TRANSMEM 5 25 Helical. {ECO:0000255}. SQ SEQUENCE 127 AA; 14803 MW; 41408F306AA89033 CRC64; MKQKILGITI AFIILLLTTV AILFSVKVKQ YLNVNLWTTQ QQNFLMFKNE KDENLFNNVS WTNFQAETTE KSAKKAFRLY KKKISTSEIS SELNKNLVKV DLSVTLEQGW YNITIMLPSK DLFEVIF // ID Y390_MYCGE Reviewed; 660 AA. AC Q49430; Q49332; Q49356; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Putative ABC transporter ATP-binding MG390; GN OrderedLocusNames=MG390; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 392-581. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00362}. CC -!- SIMILARITY: Contains 1 peptidase C39 domain. {ECO:0000255|PROSITE- CC ProRule:PRU00362}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71618.1; -; Genomic_DNA. DR EMBL; U02248; AAA03404.1; -; Genomic_DNA. DR EMBL; U02218; AAA03372.1; -; Genomic_DNA. DR PIR; B64243; B64243. DR RefSeq; WP_010869463.1; NC_000908.2. DR ProteinModelPortal; Q49430; -. DR EnsemblBacteria; AAC71618; AAC71618; MG_390. DR KEGG; mge:MG_390; -. DR PATRIC; 20010366; VBIMycGen98045_0456. DR OMA; NECGICV; -. DR OrthoDB; EOG6H1PW2; -. DR BioCyc; MGEN243273:GH2R-447-MONOMER; -. DR Proteomes; UP000000807; 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 GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005074; Peptidase_C39. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF03412; Peptidase_C39; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50990; PEPTIDASE_C39; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Protease; Reference proteome; Thiol protease; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 660 Putative ABC transporter ATP-binding FT MG390. FT /FTId=PRO_0000093247. FT TRANSMEM 150 170 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. FT TRANSMEM 265 285 Helical. {ECO:0000255}. FT TRANSMEM 290 310 Helical. {ECO:0000255}. FT TRANSMEM 379 399 Helical. {ECO:0000255}. FT TRANSMEM 402 422 Helical. {ECO:0000255}. FT DOMAIN 6 126 Peptidase C39. {ECO:0000255|PROSITE- FT ProRule:PRU00362}. FT DOMAIN 464 657 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00362}. FT NP_BIND 494 501 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00362}. FT ACT_SITE 12 12 {ECO:0000255|PROSITE-ProRule:PRU00362}. FT CONFLICT 392 392 L -> F (in Ref. 2; AAA03404). FT {ECO:0000305}. SQ SEQUENCE 660 AA; 76380 MW; 3CB9AEF9FFB89771 CRC64; MKIIYQEQQN ECGICVIGML ANAIHDEKYV HDELLEQINL PPNGLSLFEM ESYGKKFGLE INSYQLTFQE LKELDSKFII VHFKDHFVIV KNKHENSWEV YDPAKGKYLL TDEKLEKLWT GYAATVAKAF KEIPPVNKSN FFSNFFDFNL VTFYVFIELI IIGISTLLAT ASRTIITNTV DFGTAVNLVV LVVYFSCLKG LNLLLQVILQ LIRNFLFWKQ YRGYLGWIIQ SLQQKSFVYF SNKSPNQLIE RQFYLKEVLS FFNFYIPNLI ISCVVALIIG VLIGINQLEF LLIAIAQIVV NAGLFCYDFF FTKKITKKEI PYVELQNKIS LQLDENLREE QNKKRFNFLM LNFRKALLQN QNINNQKEIN RLTIENIKSF FQQGFDFAIL GLGVIGIIEQ RYQLSFLFYV FGIQSLFSTY ATRIVQFGAA INIYHYCREK LVNLFIETKK DEGIKVNWQC PDEISLENLS VTLNQHVDLA NLSLKIKNET VIFGQNGSGK STFLKILTGR GFEYTGNIKF NNVDLKRCSK EQLFENVYYL KGQNLMQTEA NDFGFSEALF NNQNPHIYQL LFDAGVQNQT KLSSGQKQIL QLFLLSNIKN KVILLDECMN AIAPEIKNRV YQLLVKPLTL NNFVVLVEHD LSFASEAQNK INLTNYLRNS // ID Y409_MYCGE Reviewed; 225 AA. AC P47649; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized protein MG409; GN OrderedLocusNames=MG409; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71637.1; -; Genomic_DNA. DR PIR; C64245; C64245. DR RefSeq; WP_009885614.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47649; -. DR STRING; 243273.MgenG_010200000445; -. DR EnsemblBacteria; AAC71637; AAC71637; MG_409. DR KEGG; mge:MG_409; -. DR PATRIC; 20010410; VBIMycGen98045_0478. DR eggNOG; COG0704; LUCA. DR KO; K02039; -. DR OMA; STWIISK; -. DR OrthoDB; EOG63FW0S; -. DR BioCyc; MGEN243273:GH2R-466-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IEA:InterPro. DR GO; GO:0045936; P:negative regulation of phosphate metabolic process; IEA:InterPro. DR InterPro; IPR028366; P_trasport_PhoU. DR InterPro; IPR026022; PhoU_dom. DR Pfam; PF01895; PhoU; 2. DR TIGRFAMs; TIGR02135; phoU_full; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 225 Uncharacterized protein MG409. FT /FTId=PRO_0000210596. SQ SEQUENCE 225 AA; 27042 MW; BBBEE44386F39195 CRC64; MENINYQILK RSEKKLLKLF FEYFKHVINA HETLNQLLCE DNLEKRKELI KTIYEMEDQS NRSEFKLINE SIWTISKNSP LASHLRLTIT IIMSSRDLER ICDYANNLTK FIEHYLHLDI KIFNNLVTLH QSALNNLKKT FESLQDKEKP LTLQFENATK TIIEFEHQYR LVLTKYYETI NKNEVTERIF LIDLVASVKH IERINDYCYN IIKSFLFIKN PEIFN // ID Y415_MYCGE Reviewed; 664 AA. AC P47655; Q2MHS8; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 2. DT 13-APR-2016, entry version 70. DE RecName: Full=Uncharacterized protein MG415; DE Flags: Precursor; GN OrderedLocusNames=MG415; ORFNames=MG_525; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP SEQUENCE REVISION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MG414/MG415 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; L43967; ABC59634.1; -; Genomic_DNA. DR PIR; I64245; I64245. DR RefSeq; WP_010869474.1; NC_000908.2. DR EnsemblBacteria; ABC59634; ABC59634; MG_525. DR KEGG; mge:MG_525; -. DR PATRIC; 20010420; VBIMycGen98045_0483. DR OrthoDB; EOG66XBH9; -. DR BioCyc; MGEN243273:GH2R-471-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 664 Uncharacterized protein MG415. FT /FTId=PRO_0000210600. FT TRANSMEM 625 645 Helical. {ECO:0000255}. SQ SEQUENCE 664 AA; 77742 MW; 79A79B7EDACC9482 CRC64; MSWKRYLKWV SFAIIPLLFA NTSIKSKLID TNLYLVKDDF QSQNQLTIAT NQLAKIIVNQ IEFDSNSLIA NPTTVLNKEL IGSKITPKLK FSDQFSNAIE MVSKLNQEFD QLANKDKTFF QFALDLLEKQ EESKFDFEPK DERIDAIFFL SNLININPKQ EKTLNFIRIL PNLIKSIFKD TTITINIKIG GKNKVITFIE NGSNVFLLSD VENFLNADQT GINFYEIEFL TFDFIVVNKT GWTLKNQPVD SFFKSVKNLP SIQKTKNGFQ YSLKFRSEYN EHHILKDHFL IPIVTNQKNF SVNDIEKNGL NSYQREQITY AIKNSFTSQK ENNLNISSAT IKYIKDPEKL IKKSLIKPSV KNGIFYVSAQ IINSNDLTKW GSKNDSEIIK DKMYFLEQNK NFPAIRTYLF QMRTKKLVLN VNDIWFKSSG DKLRVIVNNV EIDEFNPKEN NTSFFESYEV HINDYFSLAN KELLIKKLNL ALSEMNLLID KKKSSLDLFP KEIKLTTLKI NSSLHFYLNV DAIKNQLNIE VNISKNRLTS LVYDIAIKNE NELQIRTTNN YLNKYIWFDL DKKNNQKLKN ELKLFLSLKK FQFKKEPNFS LKKNSYSFQI DKIIQSNSED KKTDIIVYLI IGFSVLVLFI TVFIYFHKWN KKQKMIKNKT RDNF // ID Y425_MYCGE Reviewed; 449 AA. AC P47664; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Probable ATP-dependent RNA helicase MG425; DE EC=3.6.4.13; GN OrderedLocusNames=MG425; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-326. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC72446.1; -; Genomic_DNA. DR EMBL; U01805; AAD12332.1; -; Genomic_DNA. DR PIR; I64246; I64246. DR RefSeq; WP_009885607.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47664; -. DR STRING; 243273.MgenG_010200000340; -. DR EnsemblBacteria; AAC72446; AAC72446; MG_425. DR KEGG; mge:MG_425; -. DR PATRIC; 20010436; VBIMycGen98045_0491. DR eggNOG; ENOG4105C1J; Bacteria. DR eggNOG; COG0513; LUCA. DR OMA; QRLPQEW; -. DR OrthoDB; EOG6GBMBM; -. DR BioCyc; MGEN243273:GH2R-479-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. 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; IPR014014; RNA_helicase_DEAD_Q_motif. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; RNA-binding. FT CHAIN 1 449 Probable ATP-dependent RNA helicase FT MG425. FT /FTId=PRO_0000055114. FT DOMAIN 34 205 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 233 383 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 47 54 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 3 31 Q motif. FT MOTIF 153 156 DEID box. SQ SEQUENCE 449 AA; 51254 MW; AF45553BFA705558 CRC64; MDSTFHELGI SQTLIETLNA LHINKPTKIQ QISIPQFLSE KNLIVHSPTG TGKTAAFAIP IIEKLLKEDQ TAKPTLVIAP TRELVEQIKT TFSNIAKNKK LRIISLIGGV PAWKQIKKIK TNPQIIVGTM GRIMDLLERK AIHFSDLEHL IIDEVDLMLD RGFKKQIFNL LEQINSFKQI AVYSASYNQE AINIAKQITN NGIFIGSPEF NKDANTNNDK LIKQFVCYLF SDQKKQALYS LIKTAQVKSI IVFCDTKKLV DDLHVFLRKN ELRTFALHGD KKQFIRERNL KIFANTKQPT ILVTTDLIGR GIHVEAIDMV INYSACLNLE AYINRMGRTG RNNHKGTCVT FCTSQEKKVF LKMVEKITDN RIAECKQMEI KLIPLKNKAK TKKGGISLDC VQKIYANAKP YDRNKRVPLA SDLFKSRMRQ PEKAMQKQKI HDNDWQSNM // ID Y452_MYCGE Reviewed; 261 AA. AC P47690; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Uncharacterized protein MG452; GN OrderedLocusNames=MG452; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC72472.1; -; Genomic_DNA. DR PIR; I64249; I64249. DR RefSeq; WP_009885582.1; NZ_AAGX01000001.1. DR STRING; 243273.MgenG_010200000180; -. DR EnsemblBacteria; AAC72472; AAC72472; MG_452. DR KEGG; mge:MG_452; -. DR PATRIC; 20010494; VBIMycGen98045_0520. DR OMA; YSPARSI; -. DR OrthoDB; EOG6CVVDQ; -. DR BioCyc; MGEN243273:GH2R-505-MONOMER; -. DR Proteomes; UP000000807; 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; IPR011631; DUF1600. DR Pfam; PF07667; DUF1600; 1. DR PIRSF; PIRSF006834; UCP006834; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 261 Uncharacterized protein MG452. FT /FTId=PRO_0000210623. FT TRANSMEM 31 51 Helical. {ECO:0000255}. FT TRANSMEM 71 91 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 130 150 Helical. {ECO:0000255}. FT TRANSMEM 167 187 Helical. {ECO:0000255}. FT TRANSMEM 213 233 Helical. {ECO:0000255}. SQ SEQUENCE 261 AA; 30379 MW; 16C26ADA42D23D00 CRC64; MLIIFKDLNL VKTNNCQIIG WWKQLSLPQK TFLSFIPLFL VTSAFVLTGI VESLLTFGTI IEQIDKFTDQ TNVMLLIYAV IYTFNPKSWL LKNQQFFLSA LAYILFTFIG YNLILSIAGI AYKSTNPYKL TSSIFLHVIA PIAFFIASFI KIKHEKDVNI NMFFKSLLLF MIYPLIYGLY LVTIPYVRHY LFNGRPSTYT IYGSITNTKN NPFAWLVVFA VLFIYFPLSY LAIYLLQLKL IKKAIQPQFN LPFTLNKWKQ K // ID Y456_MYCGE Reviewed; 334 AA. AC P47694; Q49238; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Uncharacterized protein MG456; GN OrderedLocusNames=MG456; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 86-182. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC72476.1; -; Genomic_DNA. DR EMBL; U01790; AAD10612.1; -; Genomic_DNA. DR PIR; D64250; D64250. DR RefSeq; WP_009885577.1; NZ_AAGX01000001.1. DR STRING; 243273.MgenG_010200000155; -. DR PRIDE; P47694; -. DR EnsemblBacteria; AAC72476; AAC72476; MG_456. DR KEGG; mge:MG_456; -. DR PATRIC; 20010502; VBIMycGen98045_0524. DR OMA; NEIPNIA; -. DR OrthoDB; EOG67X21S; -. DR BioCyc; MGEN243273:GH2R-509-MONOMER; -. DR Proteomes; UP000000807; 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 1 334 Uncharacterized protein MG456. FT /FTId=PRO_0000210625. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT TRANSMEM 55 75 Helical. {ECO:0000255}. FT CONFLICT 181 181 F -> S (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 334 AA; 38354 MW; D142C358CE474C71 CRC64; MSDLTKFNKF FLTPNKLNAF LRVIGLCGLF SVIAISFGIY SYTRNEIPNI ASLFLIVLGS VVLFLAFVIH FAALFKRNKL LKKVNKENRT NLWQKEMGNF KAIESFEFFE QGPISSDILP SFYPTALYNF EPLPRQFKVT YKDGSEFVFG HIYAIKRSSN KTEKVACLIA ITPAINSENH FFLTDANYSL NKNVAQFEAL TENKKQENIS LFVEKDSNFS FQNLDTEVLN KVLFNPLNVY AKFNVYNDTV HTYLFMSVPT TFMDTKLKVN EAFDDLVTNI KLQASYDFKT LNSMQKVVDL LHNKLIKKPE SKSSSQKSVE TEIEKEVKDK LAKN // ID Y356_MYCGE Reviewed; 280 AA. AC Q49423; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 73. DE RecName: Full=Uncharacterized protein MG356; GN OrderedLocusNames=MG356; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71581.1; -; Genomic_DNA. DR PIR; D64239; D64239. DR RefSeq; WP_009885813.1; NZ_AAGX01000006.1. DR ProteinModelPortal; Q49423; -. DR STRING; 243273.MgenG_010200001923; -. DR EnsemblBacteria; AAC71581; AAC71581; MG_356. DR KEGG; mge:MG_356; -. DR PATRIC; 20010288; VBIMycGen98045_0418. DR eggNOG; ENOG4105I2P; Bacteria. DR eggNOG; COG0510; LUCA. DR KO; K00924; -. DR OMA; ANMARES; -. DR OrthoDB; EOG628F4J; -. DR BioCyc; MGEN243273:GH2R-410-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR InterPro; IPR002575; Aminoglycoside_PTrfase. DR InterPro; IPR011009; Kinase-like_dom. DR Pfam; PF01636; APH; 1. DR SUPFAM; SSF56112; SSF56112; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 280 Uncharacterized protein MG356. FT /FTId=PRO_0000210563. SQ SEQUENCE 280 AA; 33367 MW; 9018F2CC3F6D988E CRC64; MDLKKAVAFL CEKLQVVETD IFKIEQIHSG FTNFSFFCEL KDHSKFQIRL SRKDVILDRR NEQIILQLVE PFFSNPFVYF DVTTGNAIKR WIEGTQPKRA TDLFLCRLVE SLKKVHSVDW KPFANELLIF DPLVYFEKTK LSAFYKRLYL NLTKKHIDIP KTLCHHDATF DNLVWTPKKQ VILIDFEWSC VDNPYYEIAN IIREELTIET ANKLIDIYGG LKRKLVFETV IYVLLFAFQW TEIMPQTEAI LNYRKWVEKR LEYFLKALFP SIWKQAQKNS // ID Y364_MYCGE Reviewed; 224 AA. AC P47604; Q49476; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 64. DE RecName: Full=Uncharacterized protein MG364; GN OrderedLocusNames=MG364; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-178. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=1945886; DOI=10.1093/nar/19.21.6027; RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A random sequencing approach for placing markers on the physical map RT of Mycoplasma genitalium."; RL Nucleic Acids Res. 19:6027-6031(1991). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71591.1; -; Genomic_DNA. DR EMBL; X61520; CAA43732.1; -; Genomic_DNA. DR PIR; C64240; C64240. DR RefSeq; WP_010869449.1; NC_000908.2. DR EnsemblBacteria; AAC71591; AAC71591; MG_364. DR KEGG; mge:MG_364; -. DR PATRIC; 20010310; VBIMycGen98045_0429. DR eggNOG; ENOG4107BAW; Bacteria. DR eggNOG; ENOG410Z9X1; LUCA. DR OMA; ERDYETE; -. DR OrthoDB; EOG6MSS30; -. DR BioCyc; MGEN243273:GH2R-419-MONOMER; -. DR Proteomes; UP000000807; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 224 Uncharacterized protein MG364. FT /FTId=PRO_0000210565. FT COMPBIAS 205 216 Poly-Lys. FT CONFLICT 94 99 IQAYIT -> RYRHIF (in Ref. 2). FT {ECO:0000305}. SQ SEQUENCE 224 AA; 26361 MW; 004BCFB8DBDCF0AE CRC64; MDGGQQGSFF GLLVIVIPII LLIVFFSKKK GAQKNDFSGE GGNRSSRKDE VWKTIKQFLQ EKNERGKEII KTFVAKKPNP LHSKKDRKLF NQEIQAYITS NNLGKSEAKR YKNEQTRLMQ RELYCIYFVT KDAKSTEVDD ARIIEAEVYQ KPTKTKSTPE RLIRILGLKN FETEMQWIQP LMVREEKRKE KEEQKKLKLA ARELKKKKKK KIKKPKEIRN QKNV // ID Y376_MYCGE Reviewed; 104 AA. AC P47616; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 66. DE RecName: Full=Uncharacterized protein MG376; GN OrderedLocusNames=MG376; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71603.1; -; Genomic_DNA. DR PIR; F64241; F64241. DR RefSeq; WP_009885939.1; NZ_AAGX01000012.1. DR ProteinModelPortal; P47616; -. DR SMR; P47616; 1-103. DR STRING; 243273.MgenG_010200002931; -. DR EnsemblBacteria; AAC71603; AAC71603; MG_376. DR KEGG; mge:MG_376; -. DR PATRIC; 20010334; VBIMycGen98045_0441. DR OMA; YVIYAND; -. DR OrthoDB; EOG6K6VCZ; -. DR BioCyc; MGEN243273:GH2R-431-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR024506; DUF3217. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF11506; DUF3217; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 104 Uncharacterized protein MG376. FT /FTId=PRO_0000210578. SQ SEQUENCE 104 AA; 12231 MW; 7A3D806CB31DF0B9 CRC64; MLNCVFLEGE IESTKWSHKK TGFLVTIKQK RLFGERSFTD FFVFYANGQL AFELEAYTQK FKTISIEGIL RTYLEKRSGI WKTTIEVVKI MKPNSKVMID YQES // ID Y440_MYCGE Reviewed; 274 AA. AC P47678; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-MAY-2016, entry version 86. DE RecName: Full=Uncharacterized lipoprotein MG440; DE Flags: Precursor; GN OrderedLocusNames=MG440; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MG439/MG440 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC72460.1; 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; L43967; AAC72460.1; ALT_INIT; Genomic_DNA. DR STRING; 243273.MgenG_010200000265; -. DR EnsemblBacteria; AAC72460; AAC72460; MG_440. DR KEGG; mge:MG_440; -. DR PATRIC; 20010464; VBIMycGen98045_0505. DR OrthoDB; EOG62K24M; -. DR BioCyc; MGEN243273:GH2R-493-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001595; Lipoprotein_3. DR Pfam; PF00938; Lipoprotein_3; 1. DR ProDom; PD003276; Lipoprotein_3; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 274 Uncharacterized lipoprotein MG440. FT /FTId=PRO_0000014049. FT LIPID 26 26 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 26 26 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 274 AA; 30777 MW; 6038B2290981F4C8 CRC64; MLKKQFWTKA GIISSLMVLG SLITACSNLS SGTNFSSLNQ LRNSFSKNSE LNQDKKELVT SLRDSFEVDS KSATNVLLDA WRFSLQDEKI LEKQDPSRFV KAFGSGKSKE DVEPSTGVKG LRLVERYTQN VASIINNVIK LSSQTVTDFS FYYNSSRDFK VQIRLQATGT FDSAQAKSYL SQIGLSDSDI KDKNSISADL IFTYTPPSSN LFSKSSFDTL LRKINFNTNL RLQIIGKDEL MQKLLQSNFV GQLADQNFQD QTIDLLPYVL YSIL // ID YBEY_MYCGE Reviewed; 154 AA. AC P47628; Q49368; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 2. DT 13-APR-2016, entry version 87. DE RecName: Full=Endoribonuclease YbeY; DE EC=3.1.-.-; GN Name=ybeY; OrderedLocusNames=MG388; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-148. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the endoribonuclease YbeY family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC71615.1; 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; L43967; AAC71615.1; ALT_INIT; Genomic_DNA. DR EMBL; U02265; AAD12531.1; -; Genomic_DNA. DR PIR; I64242; I64242. DR RefSeq; WP_009885634.1; NZ_AAGX01000001.1. DR ProteinModelPortal; P47628; -. DR STRING; 243273.MgenG_010200000575; -. DR EnsemblBacteria; AAC71615; AAC71615; MG_388. DR KEGG; mge:MG_388; -. DR PATRIC; 20010362; VBIMycGen98045_0454. DR eggNOG; COG0319; LUCA. DR KO; K07042; -. DR OMA; GEIFLCP; -. DR OrthoDB; EOG6NGVW6; -. DR BioCyc; MGEN243273:GH2R-445-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.40.390.30; -; 1. DR InterPro; IPR023091; MetalPrtase_cat_dom_prd. DR InterPro; IPR002036; YbeY. DR Pfam; PF02130; UPF0054; 1. DR TIGRFAMs; TIGR00043; TIGR00043; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; KW Nuclease; Reference proteome; Ribosome biogenesis; rRNA processing; KW Zinc. FT CHAIN 1 154 Endoribonuclease YbeY. FT /FTId=PRO_0000210588. FT METAL 117 117 Zinc; catalytic. {ECO:0000250}. FT METAL 121 121 Zinc; catalytic. {ECO:0000250}. FT METAL 127 127 Zinc; catalytic. {ECO:0000250}. SQ SEQUENCE 154 AA; 17940 MW; 50B30B6D29E913B4 CRC64; MKSSFSINSS RLFKRFFGKN YQAGVELCFQ IIKSSLNLSF DPEFALLIVS CSKMKKLNKQ FLKRRGCTDV ISLCYNETET GFSLAIGEIF LCPKYIFKKA KEIGCNNWFL LTRCLIHGIL HLFEFNHEES EAFESVTMFF QDAIHEEILS VWKF // ID Y449_MYCGE Reviewed; 228 AA. AC P47687; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-APR-2016, entry version 67. DE RecName: Full=Uncharacterized protein MG449; GN OrderedLocusNames=MG449; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00209}. CC -!- SEQUENCE CAUTION: CC Sequence=L43967; Type=Frameshift; Positions=69; 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; L43967; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P47687; -. DR STRING; 243273.MgenG_010200000200; -. DR eggNOG; ENOG410837Q; Bacteria. DR eggNOG; COG0073; LUCA. DR OMA; NTHLKRC; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR002547; tRNA-bd_dom. DR Pfam; PF01588; tRNA_bind; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; RNA-binding; tRNA-binding. FT CHAIN 1 228 Uncharacterized protein MG449. FT /FTId=PRO_0000210621. FT DOMAIN 99 207 tRNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00209}. SQ SEQUENCE 228 AA; 25863 MW; 66F742DD72DECB3B CRC64; MFDISKDFVS IFYRKETLKN CMFGIIGSRS ETTLRQQNDK DWSFFVNDAN RITGFNFFNI KKSFKKFFLS HRFNEGLNYP SLKIMKRISE LLGYDLISLA NKVPFVVCEV VSVIPIANTH LKRCKVNTGL TKSLDIVCGA NNVRVGMKTV LVQVGGVLPS GTVIKKTKIA GFDSVGMLCS EKELNLKQKN EGIIEINPKI KVGKPFIDVY LNKQHSKWVN TKKRVKLS // ID Y450_MYCGE Reviewed; 237 AA. AC P47688; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 11-MAY-2016, entry version 79. DE RecName: Full=DegV domain-containing protein MG450; GN OrderedLocusNames=MG450; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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; L43967; AAC72470.1; -; Genomic_DNA. DR PIR; G64249; G64249. DR ProteinModelPortal; P47688; -. DR STRING; 243273.MgenG_010200000190; -. DR EnsemblBacteria; AAC72470; AAC72470; MG_450. DR KEGG; mge:MG_450; -. DR PATRIC; 20010490; VBIMycGen98045_0518. DR eggNOG; COG1307; LUCA. DR OrthoDB; EOG65TRSF; -. DR BioCyc; MGEN243273:GH2R-503-MONOMER; -. DR Proteomes; UP000000807; 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 1 237 DegV domain-containing protein MG450. FT /FTId=PRO_0000209773. FT DOMAIN 1 236 DegV. {ECO:0000255|PROSITE- FT ProRule:PRU00815}. FT BINDING 12 12 Fatty acid. {ECO:0000250}. FT BINDING 44 44 Fatty acid. {ECO:0000250}. SQ SEQUENCE 237 AA; 27084 MW; B19F3701F967001C CRC64; MINAPKGVKF STSQTSEEEV RDKVKSIIND YDLIIGIPID KEISTSYLNW KIVEKEFEDK FHVLDSRIVE VLIAWLISDI KVWLKNNQYS RAGLDEFVYN FRNKCGAILF VTDTKPLVAG GRLSNLKSFI IKSFKFHLLI SFLGETGKLQ FFNKAQSASS AHKLAVQFLE KKLLKKEVNF RRAALLTTMF ETDKNQLIKQ EFVTLLNNAV DVSEHLLSPV ICTHTGINSY AFLIQTE // ID YCHF_MYCGE Reviewed; 367 AA. AC P47270; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000255|HAMAP-Rule:MF_00944}; GN Name=ychF {ECO:0000255|HAMAP-Rule:MF_00944}; OrderedLocusNames=MG024; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S CC ribosomal subunit in a nucleotide-independent manner. CC {ECO:0000255|HAMAP-Rule:MF_00944}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. OBG GTPase family. YchF/OLA1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00944}. CC -!- SIMILARITY: Contains 1 OBG-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; L43967; AAC71240.1; -; Genomic_DNA. DR PIR; F64202; F64202. DR RefSeq; WP_009885916.1; NZ_AAGX01000010.1. DR ProteinModelPortal; P47270; -. DR STRING; 243273.MgenG_010200002761; -. DR EnsemblBacteria; AAC71240; AAC71240; MG_024. DR KEGG; mge:MG_024; -. DR PATRIC; 20009424; VBIMycGen98045_0022. DR eggNOG; ENOG4105C3G; Bacteria. DR eggNOG; COG0012; LUCA. DR KO; K06942; -. DR OMA; CTIEPNI; -. DR OrthoDB; EOG6NSGJC; -. DR BioCyc; MGEN243273:GH2R-24-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.150.300; -; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00944; YchF_OLA1_ATPase; 1. 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 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 367 Ribosome-binding ATPase YchF. FT /FTId=PRO_0000122458. FT DOMAIN 2 258 OBG-type G. FT NP_BIND 11 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00944}. FT METAL 15 15 Magnesium. {ECO:0000250}. FT METAL 35 35 Magnesium. {ECO:0000250}. SQ SEQUENCE 367 AA; 41198 MW; 98AFCFADDE6C9BDC CRC64; MLSAGIVGLP NVGKSTLFSA ITNLQVEIAN YPFATIEPNT GIVNVSDERL DKLASLINPE KIVYTTFRFV DIAGLVKGAS QGQGLGNQFL ANIREVDLIC HVVRCFQDKK IVHVNNTIDP VFDFEIIVNE LIQADFELIT NRIGKLKRKA ESGDKIAKEE FVLLEIVLNG LKQGQMPIQT LSESELKTIK SLNLLTAKPI LIVANVSEND LLNLDNNEAL KKLNAFLDQK KIPKAITVCS LIEKELSGLK LEQRQYFLDE LGLKNYSGLN RVIQAAYQTL NLWSFFTFGK KEVRAWTFKK GWNAPQCAGQ IHSDFEKGFI KVEVISWDQL FAMKSLQEAK KQGLIRLEGK NYLIKDGDVC NFKFNVT // ID YHIT_MYCGE Reviewed; 141 AA. AC P47378; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=Uncharacterized HIT-like protein MG132; GN OrderedLocusNames=MG132; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- SIMILARITY: Contains 1 HIT domain. {ECO:0000255|PROSITE- CC ProRule:PRU00464}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71349.1; -; Genomic_DNA. DR PIR; F64214; F64214. DR RefSeq; WP_009885688.1; NZ_AAGX01000002.1. DR ProteinModelPortal; P47378; -. DR STRING; 243273.MgenG_010200000935; -. DR EnsemblBacteria; AAC71349; AAC71349; MG_132. DR KEGG; mge:MG_132; -. DR PATRIC; 20009670; VBIMycGen98045_0144. DR eggNOG; ENOG4107Z60; Bacteria. DR eggNOG; COG0537; LUCA. DR KO; K02503; -. DR OMA; EGHILIL; -. DR OrthoDB; EOG69GZSV; -. DR BioCyc; MGEN243273:GH2R-136-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.30.428.10; -; 1. DR InterPro; IPR019808; Histidine_triad_CS. DR InterPro; IPR001310; Histidine_triad_HIT. DR InterPro; IPR011146; HIT-like. DR PANTHER; PTHR23089; PTHR23089; 1. DR Pfam; PF01230; HIT; 1. DR PRINTS; PR00332; HISTRIAD. DR SUPFAM; SSF54197; SSF54197; 1. DR PROSITE; PS00892; HIT_1; 1. DR PROSITE; PS51084; HIT_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 141 Uncharacterized HIT-like protein MG132. FT /FTId=PRO_0000109820. FT DOMAIN 10 117 HIT. {ECO:0000255|PROSITE- FT ProRule:PRU00464}. FT MOTIF 102 106 Histidine triad motif. SQ SEQUENCE 141 AA; 15587 MW; 0A0622386B036F2C CRC64; MEKNTTSSCI FCDIVQGSIT SYKIGENEHA IAFLDAFPVA DGHTLVIPKK HAVDFSSTDQ KELQAVSLLA KQIALKLKMT LKPSGLNYVS NEGAIAGQVV FHFHLHIVPK YETGKGFGYN VNKTNKRSLE ENYQLISESK N // ID YIDC_MYCGE Reviewed; 385 AA. AC P47702; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Membrane protein insertase YidC; DE AltName: Full=Foldase YidC; DE AltName: Full=Membrane integrase YidC; DE AltName: Full=Membrane protein YidC; GN Name=yidC; OrderedLocusNames=MG464; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). 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 (By similarity). {ECO:0000250}. 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 (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC 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; L43967; AAC72484.1; -; Genomic_DNA. DR PIR; C64251; C64251. DR RefSeq; WP_009885569.1; NZ_AAGX01000001.1. DR STRING; 243273.MgenG_010200000095; -. DR EnsemblBacteria; AAC72484; AAC72484; MG_464. DR KEGG; mge:MG_464; -. DR PATRIC; 20010522; VBIMycGen98045_0534. DR eggNOG; ENOG41080C2; Bacteria. DR eggNOG; COG0706; LUCA. DR KO; K03217; -. DR OMA; FKVITIC; -. DR OrthoDB; EOG67MF0Q; -. DR BioCyc; MGEN243273:GH2R-517-MONOMER; -. DR Proteomes; UP000000807; 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 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 membrane; Chaperone; Complete proteome; Membrane; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 385 Membrane protein insertase YidC. FT /FTId=PRO_0000124724. FT TRANSMEM 39 59 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 150 170 Helical. {ECO:0000255}. FT TRANSMEM 222 242 Helical. {ECO:0000255}. FT TRANSMEM 247 267 Helical. {ECO:0000255}. FT TRANSMEM 270 290 Helical. {ECO:0000255}. FT TRANSMEM 325 345 Helical. {ECO:0000255}. SQ SEQUENCE 385 AA; 44207 MW; BCB2964F7842893A CRC64; MPIKLAQTNK EIKTTFNPFW SAAVVNEKNN WKNFKKFSAI FIKVIKVFIF IFLTIVGLWG CTQTLAQPWT GTNQVLGSGL EIGYKFGTTG DYRYDLISNN FGPYFTFSDY TLAYGPFYGW FVWPAAQIVL PIMYATRVPL GSGVELGFNM ILSLIVLLLL VRLITIVITL NSTLALEKMN EVQGKLAEIN AKYKGAIDLQ SKRNRQLEIM SLYKKHNIKS SAAFVQVFVT LPIFLIIYRI VTTLRPIKAI ILFNFWDLSK VPLTEIFSNF TTTGWPFIIF LVIVLPVQFL SQKLPQVWAS KRNENAKAHS QKSIEQLNKT KKMQLIFYFV FAAITAFSAA GVGVYWFLNA LFTLLQSYLT HVFIVKRREK RKQNYSKLDL ILERE // ID YQGF_MYCGE Reviewed; 138 AA. AC Q9ZB76; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=Putative pre-16S rRNA nuclease {ECO:0000255|HAMAP-Rule:MF_00651}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00651}; GN OrderedLocusNames=MG291.1; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP IDENTIFICATION. RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Could be a nuclease involved in processing of the 5'-end CC of pre-16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00651}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00651}. CC -!- SIMILARITY: Belongs to the YqgF nuclease family. CC {ECO:0000255|HAMAP-Rule:MF_00651}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L43967; AAC71518.1; -; Genomic_DNA. DR RefSeq; WP_010869411.1; NZ_AAGX01000008.1. DR ProteinModelPortal; Q9ZB76; -. DR STRING; 243273.MgenG_010200002399; -. DR PRIDE; Q9ZB76; -. DR EnsemblBacteria; AAC71518; AAC71518; MG_505. DR KEGG; mge:MG_505; -. DR PATRIC; 20010112; VBIMycGen98045_0342. DR eggNOG; COG0816; LUCA. DR KO; K07447; -. DR OMA; NTIDRFP; -. DR OrthoDB; EOG6N94FV; -. DR BioCyc; MGEN243273:GH2R-327-MONOMER; -. DR Proteomes; UP000000807; 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:0000967; P:rRNA 5'-end processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.140; -; 1. DR HAMAP; MF_00651; Nuclease_YqgF; 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. DR TIGRFAMs; TIGR00250; RNAse_H_YqgF; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Nuclease; Reference proteome; KW Ribosome biogenesis. FT CHAIN 1 138 Putative pre-16S rRNA nuclease. FT /FTId=PRO_0000172091. SQ SEQUENCE 138 AA; 16064 MW; 56105E08C1C0B910 CRC64; MKYILAIDFG LKKIGTAIAN TLDKYPSAFH VFEVKNNFKT AVNNLFLRIK NDGYELEKIV IGFPKFHYYS DIQKAIKSFK QLLEKRFNLP IILVDESNTT SAVKDKLITM DLKHKDFKKA KDTLAAVLIL ERFFQNYH //